Microtubule Interactions
Published by Anonymous on 2007/9/28 (3487 reads)
1: Curr Opin Struct Biol. 2007 Apr;17(2):253-9. Epub 2007 Mar 26.
Structural insights into microtubule doublet interactions in axonemes.
Downing KH, Sui H.
Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. khdowning@lbl.gov
Coordinated sliding of microtubule doublets, driven by dynein motors, produces periodic beating of eukaryotic cilia and flagella. Recent structural studies of the axoneme, which forms the core of cilia and flagella, have used cryo-electron tomography to reveal new details of the interactions between some of the multitude of proteins that form the axoneme and regulate its movement. Connections between the several types of dyneins, in particular, suggest ways in which their action might be coordinated. Study of the molecular architecture of isolated doublets has provided a structural basis for understanding mechanical properties related to the bending of the axoneme, and has also offered insight into the potential role of doublets in the mechanism of dynein activity regulation.
Publication Types:
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Review
PMID: 17387011 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Cell Mol Life Sci. 2007 Feb;64(3):307-17.
Action and interactions at microtubule ends.
Morrison EE.
CRUK Clinical Centre at Leeds, Leeds Institute of Molecular Medicine, St James's University Hospital, Leeds LS9 7TF, United Kingdom. ewan.morrison@cancer.org.uk
Microtubule dynamic instability is fundamentally important to the way cells respond to their environment and segregate their genetic material. A disparate class of proteins defined by their localisation to growing microtubule plus ends ('+TIPS') play a key role in controlling microtubule dynamics and organisation. They directly impact upon the behaviour of the microtubule tip and link this structure to interfaces that include kinetochores and the cortex of the cell. Surprisingly, some +TIPs also have important functions at the microtubule minus end. These properties contribute to the important roles played by +TIPs in processes such as mitosis and cell migration. This review examines how recent advances have impacted our understanding of +TIP function in mammalian cells, with emphasis on the emergence of the EB1 family as a core component of +TIP activities. An overview of the use of +TIP imaging as a tool for the cell biologist is also presented.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 17221167 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Curr Opin Cell Biol. 2005 Feb;17(1):35-46.
Kinetochore-spindle microtubule interactions during mitosis.
Kline-Smith SL, Sandall S, Desai A.
Ludwig Institute for Cancer Research, Department of Cellular & Molecular Medicine, University of California, San Diego, 9500 Gilman Dr, CMM-East, Rm 3080, La Jolla, California 92093, USA.
The kinetochore is a proteinaceous structure that assembles onto centromeric DNA and mediates chromosome attachment to microtubules during mitosis. This description is deceivingly simple: recent proteomic studies suggest that the diminutive kinetochores of Saccharomyces cerevisiae are comprised of at least 60 proteins organized into as many as 14 different subcomplexes. Many of these proteins, such as the centromeric histone variant CENP-A, and entire subcomplexes, such as the Ndc80(Hec1) complex, are conserved from yeast to humans despite the diverse nature of the DNA sequences on which they assemble. There have recently been advances in our understanding of the molecular basis of how kinetochores establish dynamic attachments to spindle microtubules, and how these attachments are correctly oriented to ensure segregation of sister chromatids to daughter cells.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 15661517 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Chromosome Res. 2004;12(6):585-97.
Kinetochore-microtubule interactions during cell division.
Maiato H, Sunkel CE.
Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal.
Proper segregation of chromosomes during cell division is essential for the maintenance of genetic stability. During this process chromosomes must establish stable functional interactions with microtubules through the kinetochore, a specialized protein structure located on the surface of the centromeric heterochromatin. Stable attachment of kinetochores to a number of microtubules results in the formation of a kinetochore fibre that mediates chromosome movement. How the kinetochore fibre is formed and how chromosome motion is produced and regulated remain major questions in cell biology. Here we look at some of the history of research devoted to the study of kinetochore-microtubule interaction and attempt to identify significant advances in the knowledge of the basic processes. Ultrastructural work has provided substantial insights into the structure of the kinetochore and associated microtubules during different stages of mitosis. Also, recent in-vivo studies have probed deep into the dynamics of kinetochore-attached microtubules suggesting possible models for the way in which kinetochores harness the capacity of microtubules to do work and turn it into chromosome motion. Much of the research in recent years suggests that indeed multiple mechanisms are involved in both formation of the k-fibre and chromosome motion. Thus, rather than moving to a unified theory, it has become apparent that most cell types have the capacity to build the spindle using multiple and probably redundant mechanisms.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 15289665 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Curr Top Med Chem. 2004;4(2):203-17.
3D QSAR models of interactions between beta-tubulin and microtubule stabilizing antimitotic agents (MSAA): a survey on taxanes and epothilones.
Manetti F, Maccari L, Corelli F, Botta M.
Dipartimento Farmaco Chimico Tecnologico, Università degli Studi di Siena, Via Aldo Moro, I-53100 Siena, Italy.
In the last two decades, paclitaxel (Taxol), 1) has dominated the anticancer chemotherapy as one of the most important antimitotic agents. Despite its clinical success, it presents some limitations due to its low aqueous solubility or multidrug-resistance (MDR) susceptibility. Among new compounds sharing paclitaxel's mechanism of action, epothilones have emerged as very promising candidates and are currently under clinical trials. While the electron crystallography (EC) structure of tubulin with embedded paclitaxel is available, only hypotheses about epothilone binding upon the protein may be advanced. This review illustrates our efforts in the minireceptor modeling approach as the most recent advances in the field of three-dimensional quantitative structure-activity relationship (3D QSAR) studies involving taxanes, epothilones and the corresponding protein environment.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 14754454 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Nat Cell Biol. 2003 Jul;5(7):599-609.
Conserved microtubule-actin interactions in cell movement and morphogenesis.
Rodriguez OC, Schaefer AW, Mandato CA, Forscher P, Bement WM, Waterman-Storer CM.
Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
Interactions between microtubules and actin are a basic phenomenon that underlies many fundamental processes in which dynamic cellular asymmetries need to be established and maintained. These are processes as diverse as cell motility, neuronal pathfinding, cellular wound healing, cell division and cortical flow. Microtubules and actin exhibit two mechanistic classes of interactions--regulatory and structural. These interactions comprise at least three conserved 'mechanochemical activity modules' that perform similar roles in these diverse cell functions.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 12833063 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Immunol Rev. 2002 Nov;189:84-97.
Regulation of microtubule-organizing center orientation and actomyosin cytoskeleton rearrangement during immune interactions.
Sancho D, Vicente-Manzanares M, Mittelbrunn M, Montoya MC, Gordón-Alonso M, Serrador JM, Sánchez-Madrid F.
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, Madrid, Spain.
The reorganization of membrane, cytoskeletal and signaling molecules during immune interactions is critical for the generation of immune response. At the initiation of the T cell-antigen presenting cell (APC) interaction, antigen-independent weak adhesion forces allow the scanning of the APC surface by the T cell receptor for specific antigens. The stabilization of T cell-APC conjugates involves the segregation of membrane and intracellular signaling proteins, driven by reorganization of membrane microdomains and cytoskeletal changes. In early T cell-APC cognate interactions, the microtubular cytoskeleton undergoes drastic changes that lead to microtubule-organizing center (MTOC) reorientation to the vicinity of the cell-cell contact area. Recent data on the dynamics of MTOC redistribution and its influence in T cell-APC conjugate stabilization, together with the description of an increasing number of signaling molecules associated to this complex, underscore the key role of MTOC translocation in the T cell response. We focus on the mechanisms that control the early MTOC reorientation during T cell-APC interaction and the relevance of this process to T cell activation.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 12445267 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: Annu Rev Cell Dev Biol. 2002;18:193-219. Epub 2002 Apr 2.
Chromosome-microtubule interactions during mitosis.
McIntosh JR, Grishchuk EL, West RR.
Department of Molecular Cellular and Developmental Biology, University of Colorado, Boulder 80309-0347, USA. richard.mcintosh@colorado.edu
Spindle microtubules interact with mitotic chromosomes, binding to their kinetochores to generate forces that are important for accurate chromosome segregation. Motor enzymes localized both at kinetochores and spindle poles help to form the biologically significant attachments between spindle fibers and their cargo, but microtubule-associated proteins without motor activity contribute to these junctions in important ways. This review examines the molecules necessary for chromosome-microtubule interaction in a range of well-studied organisms, using biological diversity to identify the factors that are essential for organized chromosome movement. We conclude that microtubule dynamics and the proteins that control them are likely to be more important for mitosis than the current enthusiasm for motor enzymes would suggest.
Publication Types:
Review
PMID: 12142285 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: Cardiovasc Pathol. 2002 May-Jun;11(3):135-40.
Microtubule-actin interactions may regulate endothelial integrity and repair.
Lee JS, Gotlieb AI.
Department of Pathology, University Health Network, University of Toronto, Ontario, Canada.
An important mechanism for the initiation and progression of atherosclerosis is the loss of endothelial integrity, which is required for normal blood vessel function. The important components of the endothelial cell cytoskeleton system that regulate endothelial integrity include actin microfilaments and microtubules, which are both associated with protein complexes that regulate cell-cell and cell-substratum adhesion. To date, studies have shown that microfilaments are essential in maintaining the structural integrity of the endothelium while microtubules regulate the directional cell migration during repair. When microtubules are disrupted at the onset of wounding, neither centrosome reorientation, which is essential for efficient endothelial cell wound repair, nor cell migration occurs. Disruption of microfilaments is also associated with inefficient endothelial cell migration and repair. How then might these systems be associated with one another? Linker proteins, which may facilitate interaction between microtubules and actin microfilaments, have recently been identified in nonendothelial systems. It is likely that microtubule-microfilament interactions are important in the complex regulation of endothelial integrity and repair especially as they relate to atherosclerotic plaque formation.
Publication Types:
Review
PMID: 12031763 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: Methods Mol Biol. 2001;161:229-39.
Xenopus egg extracts as a model system for analysis of microtubule, actin filament, and intermediate filament interactions.
Mandato CA, Weber KL, Zandy AJ, Keating TJ, Bement WM.
Department of Zoology, University of Wisconsin, Madison, WI, USA.
Publication Types:
Review
PMID: 11190509 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: Cell Motil Cytoskeleton. 2000 Feb;45(2):87-92.
Microtubule-actomyosin interactions in cortical flow and cytokinesis.
Mandato CA, Benink HA, Bement WM.
Department of Zoology, University of Wisconsin, Madison, WI 53706, USA.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 10658205 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
12: Curr Opin Cell Biol. 1999 Feb;11(1):34-44.
Structures of kinesin and kinesin-microtubule interactions.
Mandelkow E, Hoenger A.
Max-Planck-Unit for Structural Molecular Biology Notkestrasse 85 D-22607 Hamburg Germany. mand@mpasmb.desy.de
Several X-ray crystal structures of kinesin motor domains have recently been solved at high resolution ( approximately 0.2-0.3 nm), in both their monomeric and dimeric states. They show the folding of the polypeptide chain and different arrangements of subunits in the dimer. In addition, cryo-electron microscopy and image reconstruction have revealed microtubules decorated with kinesin at intermediate resolution ( approximately 2 nm), showing the distribution and orientation of kinesin heads on the microtubule surface. The comparison of the X-ray and electron microscopy results yields a model of how monomeric motor domains bind to the microtubule but the binding of dimeric motors, their stoichiometry, or the influence of nucleotides remains a matter of debate.
Publication Types:
Review
PMID: 10047529 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
13: Curr Opin Cell Biol. 1999 Feb;11(1):61-7.
Positive feedback interactions between microtubule and actin dynamics during cell motility.
Waterman-Storer CM, Salmon E.
Department of Biology 607 Fordham Hall University of North Carolina Chapel Hill NC 27599-3280 USA. waterman@email.unc.edu
The migration of tissue cells requires interplay between the microtubule and actin cytoskeletal systems. Recent reports suggest that interactions of microtubules with actin dynamics creates a polarization of microtubule assembly behavior in cells, such that microtubule growth occurs at the leading edge and microtubule shortening occurs at the cell body and rear. Microtubule growth and shortening may activate Rac1 and RhoA signaling, respectively, to control actin dynamics. Thus, an actin-dependent gradient in microtubule dynamic-instability parameters in cells may feed back through the activation of specific signalling pathways to perpetuate the polarized actin-assembly dynamics required for cell motility.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 10047528 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
14: Ann N Y Acad Sci. 1996 Jan 17;777:96-106.
Structure, microtubule interactions, and phosphorylation of tau protein.
Mandelkow EM, Schweers O, Drewes G, Biernat J, Gustke N, Trinczek B, Mandelkow E.
Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany. mand@mpasmb.desy.de
This paper summarizes recent structural and functional studies on tau protein, its interactions with microtubules, its self-assembly into paired helical filaments (PHF)-like fibers, and its modification by phosphorylation. The structure of tau in solution resembles that of a random coil. Both tau and Alzheimer PHFs have very little secondary structure, making it improbable that the assembly of tau into PHFs is based on interacting beta sheets. Tau's binding to microtubules can be described by a "jaws" effect. The domain containing the repeats binds very weakly, while the flanking regions (jaws) bind strongly, even without the repeats. However, only the combination of flanking regions and repeats makes binding productive in terms of microtubule nucleation and assembly. Although the majority of Alzheimer-like phosphorylation sites are outside the repeats they have only a weak influence on binding, whereas the phosphorylation at Ser262 inside the repeats inhibits binding and makes microtubules dynamically unstable. This site can be phosphorylated by kinases present in brain tissue, and it is uniquely phosphorylated in Alzheimer brain.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 8624133 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
15: Methods Cell Biol. 1993;39:277-92.
The diatom central spindle as a model system for studying antiparallel microtubule interactions during spindle elongation in vitro.
Hogan CJ, Neale PJ, Lee M, Cande WZ.
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Publication Types:
Review
PMID: 8246804 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
16: Cell Motil Cytoskeleton. 1990;16(2):99-103.
Antiparallel microtubule interactions: spindle formation and anaphase B.
Hogan CJ, Cande WZ.
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2198114 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
17: Int Rev Cytol. 1981;72:1-47.
Microtubule-membrane interactions in cilia and flagella.
Dentler WL.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 7019129 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
18: Horm Metab Res Suppl. 1980;Suppl 10:163-7.
Microtubule interactions in islets of Langerhans.
Pipeleers DG, Harnie N, Heylen L, Wauters G.
Morphologic and functional studies have implicated islet microtubules in the transport of the B-cell secretory product form the endoplasmic reticulum to the peripheral pool of secretory vesicles. The participation of the microtubular apparatus in the insulin release mechanism appears to be mediated through an increased rate of tubulin synthesis and of tubulin polymerization, two possible sites for a physiologic and pharmacologic regulation of hormone discharge. It is conceivable that cytoplasmic microtubules from either a rigid cytoskeleton which facilitates hormone transport by establishing n intracellular organization or act as a motion generating system along which the secretory vesicles are actively transported to the cell periphery. The existence of an eventual interaction between secretory vesicles and islet microtubules has been examined by measuring I123-tubulin binding to various subcellular fractions. In working out the experimental procedure on liver tissue, tubulin was found to bind to all subcellular fractions being most pronounced in the microsomial fraction; in the cytosol, tubulin was incorporated into high molecular weight complexes. Similar results were obtained with islet subcellular fractions, binding per microgram protein being tenfold higher than in liver tissue. In view of the calcium-induced increase in tubulin binding to islet subcellular fractions, and of the high affinity of tubulin and secretory vesicles for calcium, it is suggested that a calcium stimulated bridge - eventually microfilamentous in nature - might link the growing microtubules to the secretory vesicles and could, as such, participate in the intracellular transport of the secretory product.
Publication Types:
In Vitro
Research Support, Non-U.S. Gov't
Review
PMID: 7005058 [PubMed - indexed for MEDLINE]
Structural insights into microtubule doublet interactions in axonemes.
Downing KH, Sui H.
Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. khdowning@lbl.gov
Coordinated sliding of microtubule doublets, driven by dynein motors, produces periodic beating of eukaryotic cilia and flagella. Recent structural studies of the axoneme, which forms the core of cilia and flagella, have used cryo-electron tomography to reveal new details of the interactions between some of the multitude of proteins that form the axoneme and regulate its movement. Connections between the several types of dyneins, in particular, suggest ways in which their action might be coordinated. Study of the molecular architecture of isolated doublets has provided a structural basis for understanding mechanical properties related to the bending of the axoneme, and has also offered insight into the potential role of doublets in the mechanism of dynein activity regulation.
Publication Types:
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Review
PMID: 17387011 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Cell Mol Life Sci. 2007 Feb;64(3):307-17.
Action and interactions at microtubule ends.
Morrison EE.
CRUK Clinical Centre at Leeds, Leeds Institute of Molecular Medicine, St James's University Hospital, Leeds LS9 7TF, United Kingdom. ewan.morrison@cancer.org.uk
Microtubule dynamic instability is fundamentally important to the way cells respond to their environment and segregate their genetic material. A disparate class of proteins defined by their localisation to growing microtubule plus ends ('+TIPS') play a key role in controlling microtubule dynamics and organisation. They directly impact upon the behaviour of the microtubule tip and link this structure to interfaces that include kinetochores and the cortex of the cell. Surprisingly, some +TIPs also have important functions at the microtubule minus end. These properties contribute to the important roles played by +TIPs in processes such as mitosis and cell migration. This review examines how recent advances have impacted our understanding of +TIP function in mammalian cells, with emphasis on the emergence of the EB1 family as a core component of +TIP activities. An overview of the use of +TIP imaging as a tool for the cell biologist is also presented.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 17221167 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Curr Opin Cell Biol. 2005 Feb;17(1):35-46.
Kinetochore-spindle microtubule interactions during mitosis.
Kline-Smith SL, Sandall S, Desai A.
Ludwig Institute for Cancer Research, Department of Cellular & Molecular Medicine, University of California, San Diego, 9500 Gilman Dr, CMM-East, Rm 3080, La Jolla, California 92093, USA.
The kinetochore is a proteinaceous structure that assembles onto centromeric DNA and mediates chromosome attachment to microtubules during mitosis. This description is deceivingly simple: recent proteomic studies suggest that the diminutive kinetochores of Saccharomyces cerevisiae are comprised of at least 60 proteins organized into as many as 14 different subcomplexes. Many of these proteins, such as the centromeric histone variant CENP-A, and entire subcomplexes, such as the Ndc80(Hec1) complex, are conserved from yeast to humans despite the diverse nature of the DNA sequences on which they assemble. There have recently been advances in our understanding of the molecular basis of how kinetochores establish dynamic attachments to spindle microtubules, and how these attachments are correctly oriented to ensure segregation of sister chromatids to daughter cells.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 15661517 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Chromosome Res. 2004;12(6):585-97.
Kinetochore-microtubule interactions during cell division.
Maiato H, Sunkel CE.
Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal.
Proper segregation of chromosomes during cell division is essential for the maintenance of genetic stability. During this process chromosomes must establish stable functional interactions with microtubules through the kinetochore, a specialized protein structure located on the surface of the centromeric heterochromatin. Stable attachment of kinetochores to a number of microtubules results in the formation of a kinetochore fibre that mediates chromosome movement. How the kinetochore fibre is formed and how chromosome motion is produced and regulated remain major questions in cell biology. Here we look at some of the history of research devoted to the study of kinetochore-microtubule interaction and attempt to identify significant advances in the knowledge of the basic processes. Ultrastructural work has provided substantial insights into the structure of the kinetochore and associated microtubules during different stages of mitosis. Also, recent in-vivo studies have probed deep into the dynamics of kinetochore-attached microtubules suggesting possible models for the way in which kinetochores harness the capacity of microtubules to do work and turn it into chromosome motion. Much of the research in recent years suggests that indeed multiple mechanisms are involved in both formation of the k-fibre and chromosome motion. Thus, rather than moving to a unified theory, it has become apparent that most cell types have the capacity to build the spindle using multiple and probably redundant mechanisms.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 15289665 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Curr Top Med Chem. 2004;4(2):203-17.
3D QSAR models of interactions between beta-tubulin and microtubule stabilizing antimitotic agents (MSAA): a survey on taxanes and epothilones.
Manetti F, Maccari L, Corelli F, Botta M.
Dipartimento Farmaco Chimico Tecnologico, Università degli Studi di Siena, Via Aldo Moro, I-53100 Siena, Italy.
In the last two decades, paclitaxel (Taxol), 1) has dominated the anticancer chemotherapy as one of the most important antimitotic agents. Despite its clinical success, it presents some limitations due to its low aqueous solubility or multidrug-resistance (MDR) susceptibility. Among new compounds sharing paclitaxel's mechanism of action, epothilones have emerged as very promising candidates and are currently under clinical trials. While the electron crystallography (EC) structure of tubulin with embedded paclitaxel is available, only hypotheses about epothilone binding upon the protein may be advanced. This review illustrates our efforts in the minireceptor modeling approach as the most recent advances in the field of three-dimensional quantitative structure-activity relationship (3D QSAR) studies involving taxanes, epothilones and the corresponding protein environment.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 14754454 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Nat Cell Biol. 2003 Jul;5(7):599-609.
Conserved microtubule-actin interactions in cell movement and morphogenesis.
Rodriguez OC, Schaefer AW, Mandato CA, Forscher P, Bement WM, Waterman-Storer CM.
Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
Interactions between microtubules and actin are a basic phenomenon that underlies many fundamental processes in which dynamic cellular asymmetries need to be established and maintained. These are processes as diverse as cell motility, neuronal pathfinding, cellular wound healing, cell division and cortical flow. Microtubules and actin exhibit two mechanistic classes of interactions--regulatory and structural. These interactions comprise at least three conserved 'mechanochemical activity modules' that perform similar roles in these diverse cell functions.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 12833063 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Immunol Rev. 2002 Nov;189:84-97.
Regulation of microtubule-organizing center orientation and actomyosin cytoskeleton rearrangement during immune interactions.
Sancho D, Vicente-Manzanares M, Mittelbrunn M, Montoya MC, Gordón-Alonso M, Serrador JM, Sánchez-Madrid F.
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, Madrid, Spain.
The reorganization of membrane, cytoskeletal and signaling molecules during immune interactions is critical for the generation of immune response. At the initiation of the T cell-antigen presenting cell (APC) interaction, antigen-independent weak adhesion forces allow the scanning of the APC surface by the T cell receptor for specific antigens. The stabilization of T cell-APC conjugates involves the segregation of membrane and intracellular signaling proteins, driven by reorganization of membrane microdomains and cytoskeletal changes. In early T cell-APC cognate interactions, the microtubular cytoskeleton undergoes drastic changes that lead to microtubule-organizing center (MTOC) reorientation to the vicinity of the cell-cell contact area. Recent data on the dynamics of MTOC redistribution and its influence in T cell-APC conjugate stabilization, together with the description of an increasing number of signaling molecules associated to this complex, underscore the key role of MTOC translocation in the T cell response. We focus on the mechanisms that control the early MTOC reorientation during T cell-APC interaction and the relevance of this process to T cell activation.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 12445267 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: Annu Rev Cell Dev Biol. 2002;18:193-219. Epub 2002 Apr 2.
Chromosome-microtubule interactions during mitosis.
McIntosh JR, Grishchuk EL, West RR.
Department of Molecular Cellular and Developmental Biology, University of Colorado, Boulder 80309-0347, USA. richard.mcintosh@colorado.edu
Spindle microtubules interact with mitotic chromosomes, binding to their kinetochores to generate forces that are important for accurate chromosome segregation. Motor enzymes localized both at kinetochores and spindle poles help to form the biologically significant attachments between spindle fibers and their cargo, but microtubule-associated proteins without motor activity contribute to these junctions in important ways. This review examines the molecules necessary for chromosome-microtubule interaction in a range of well-studied organisms, using biological diversity to identify the factors that are essential for organized chromosome movement. We conclude that microtubule dynamics and the proteins that control them are likely to be more important for mitosis than the current enthusiasm for motor enzymes would suggest.
Publication Types:
Review
PMID: 12142285 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: Cardiovasc Pathol. 2002 May-Jun;11(3):135-40.
Microtubule-actin interactions may regulate endothelial integrity and repair.
Lee JS, Gotlieb AI.
Department of Pathology, University Health Network, University of Toronto, Ontario, Canada.
An important mechanism for the initiation and progression of atherosclerosis is the loss of endothelial integrity, which is required for normal blood vessel function. The important components of the endothelial cell cytoskeleton system that regulate endothelial integrity include actin microfilaments and microtubules, which are both associated with protein complexes that regulate cell-cell and cell-substratum adhesion. To date, studies have shown that microfilaments are essential in maintaining the structural integrity of the endothelium while microtubules regulate the directional cell migration during repair. When microtubules are disrupted at the onset of wounding, neither centrosome reorientation, which is essential for efficient endothelial cell wound repair, nor cell migration occurs. Disruption of microfilaments is also associated with inefficient endothelial cell migration and repair. How then might these systems be associated with one another? Linker proteins, which may facilitate interaction between microtubules and actin microfilaments, have recently been identified in nonendothelial systems. It is likely that microtubule-microfilament interactions are important in the complex regulation of endothelial integrity and repair especially as they relate to atherosclerotic plaque formation.
Publication Types:
Review
PMID: 12031763 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: Methods Mol Biol. 2001;161:229-39.
Xenopus egg extracts as a model system for analysis of microtubule, actin filament, and intermediate filament interactions.
Mandato CA, Weber KL, Zandy AJ, Keating TJ, Bement WM.
Department of Zoology, University of Wisconsin, Madison, WI, USA.
Publication Types:
Review
PMID: 11190509 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: Cell Motil Cytoskeleton. 2000 Feb;45(2):87-92.
Microtubule-actomyosin interactions in cortical flow and cytokinesis.
Mandato CA, Benink HA, Bement WM.
Department of Zoology, University of Wisconsin, Madison, WI 53706, USA.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 10658205 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
12: Curr Opin Cell Biol. 1999 Feb;11(1):34-44.
Structures of kinesin and kinesin-microtubule interactions.
Mandelkow E, Hoenger A.
Max-Planck-Unit for Structural Molecular Biology Notkestrasse 85 D-22607 Hamburg Germany. mand@mpasmb.desy.de
Several X-ray crystal structures of kinesin motor domains have recently been solved at high resolution ( approximately 0.2-0.3 nm), in both their monomeric and dimeric states. They show the folding of the polypeptide chain and different arrangements of subunits in the dimer. In addition, cryo-electron microscopy and image reconstruction have revealed microtubules decorated with kinesin at intermediate resolution ( approximately 2 nm), showing the distribution and orientation of kinesin heads on the microtubule surface. The comparison of the X-ray and electron microscopy results yields a model of how monomeric motor domains bind to the microtubule but the binding of dimeric motors, their stoichiometry, or the influence of nucleotides remains a matter of debate.
Publication Types:
Review
PMID: 10047529 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
13: Curr Opin Cell Biol. 1999 Feb;11(1):61-7.
Positive feedback interactions between microtubule and actin dynamics during cell motility.
Waterman-Storer CM, Salmon E.
Department of Biology 607 Fordham Hall University of North Carolina Chapel Hill NC 27599-3280 USA. waterman@email.unc.edu
The migration of tissue cells requires interplay between the microtubule and actin cytoskeletal systems. Recent reports suggest that interactions of microtubules with actin dynamics creates a polarization of microtubule assembly behavior in cells, such that microtubule growth occurs at the leading edge and microtubule shortening occurs at the cell body and rear. Microtubule growth and shortening may activate Rac1 and RhoA signaling, respectively, to control actin dynamics. Thus, an actin-dependent gradient in microtubule dynamic-instability parameters in cells may feed back through the activation of specific signalling pathways to perpetuate the polarized actin-assembly dynamics required for cell motility.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 10047528 [PubMed - indexed for MEDLINE]
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14: Ann N Y Acad Sci. 1996 Jan 17;777:96-106.
Structure, microtubule interactions, and phosphorylation of tau protein.
Mandelkow EM, Schweers O, Drewes G, Biernat J, Gustke N, Trinczek B, Mandelkow E.
Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany. mand@mpasmb.desy.de
This paper summarizes recent structural and functional studies on tau protein, its interactions with microtubules, its self-assembly into paired helical filaments (PHF)-like fibers, and its modification by phosphorylation. The structure of tau in solution resembles that of a random coil. Both tau and Alzheimer PHFs have very little secondary structure, making it improbable that the assembly of tau into PHFs is based on interacting beta sheets. Tau's binding to microtubules can be described by a "jaws" effect. The domain containing the repeats binds very weakly, while the flanking regions (jaws) bind strongly, even without the repeats. However, only the combination of flanking regions and repeats makes binding productive in terms of microtubule nucleation and assembly. Although the majority of Alzheimer-like phosphorylation sites are outside the repeats they have only a weak influence on binding, whereas the phosphorylation at Ser262 inside the repeats inhibits binding and makes microtubules dynamically unstable. This site can be phosphorylated by kinases present in brain tissue, and it is uniquely phosphorylated in Alzheimer brain.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 8624133 [PubMed - indexed for MEDLINE]
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15: Methods Cell Biol. 1993;39:277-92.
The diatom central spindle as a model system for studying antiparallel microtubule interactions during spindle elongation in vitro.
Hogan CJ, Neale PJ, Lee M, Cande WZ.
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Publication Types:
Review
PMID: 8246804 [PubMed - indexed for MEDLINE]
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16: Cell Motil Cytoskeleton. 1990;16(2):99-103.
Antiparallel microtubule interactions: spindle formation and anaphase B.
Hogan CJ, Cande WZ.
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2198114 [PubMed - indexed for MEDLINE]
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17: Int Rev Cytol. 1981;72:1-47.
Microtubule-membrane interactions in cilia and flagella.
Dentler WL.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 7019129 [PubMed - indexed for MEDLINE]
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18: Horm Metab Res Suppl. 1980;Suppl 10:163-7.
Microtubule interactions in islets of Langerhans.
Pipeleers DG, Harnie N, Heylen L, Wauters G.
Morphologic and functional studies have implicated islet microtubules in the transport of the B-cell secretory product form the endoplasmic reticulum to the peripheral pool of secretory vesicles. The participation of the microtubular apparatus in the insulin release mechanism appears to be mediated through an increased rate of tubulin synthesis and of tubulin polymerization, two possible sites for a physiologic and pharmacologic regulation of hormone discharge. It is conceivable that cytoplasmic microtubules from either a rigid cytoskeleton which facilitates hormone transport by establishing n intracellular organization or act as a motion generating system along which the secretory vesicles are actively transported to the cell periphery. The existence of an eventual interaction between secretory vesicles and islet microtubules has been examined by measuring I123-tubulin binding to various subcellular fractions. In working out the experimental procedure on liver tissue, tubulin was found to bind to all subcellular fractions being most pronounced in the microsomial fraction; in the cytosol, tubulin was incorporated into high molecular weight complexes. Similar results were obtained with islet subcellular fractions, binding per microgram protein being tenfold higher than in liver tissue. In view of the calcium-induced increase in tubulin binding to islet subcellular fractions, and of the high affinity of tubulin and secretory vesicles for calcium, it is suggested that a calcium stimulated bridge - eventually microfilamentous in nature - might link the growing microtubules to the secretory vesicles and could, as such, participate in the intracellular transport of the secretory product.
Publication Types:
In Vitro
Research Support, Non-U.S. Gov't
Review
PMID: 7005058 [PubMed - indexed for MEDLINE]
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