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Actin Structure
Published by Anonymous on 2007/9/28 (2042 reads)
1: Adv Exp Med Biol. 2007;592:385-401.


Modeling of the F-actin structure.

Oda T, Stegmann H, Schröder RR, Namba K, Maéda Y.

RIKEN Harima Institute, RIKEN SPring-8 center, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan. toda@spring8.or.jp

Publication Types:
Comparative Study
Review

PMID: 17278381 [PubMed - indexed for MEDLINE]

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2: Tanpakushitsu Kakusan Koso. 2006 May;51(6 Suppl):505-10.


[Structure and function of actin]

[Article in Japanese]

Nakagawa H, Miyamoto S.

Publication Types:
Review

PMID: 16719304 [PubMed - indexed for MEDLINE]

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3: Sheng Li Ke Xue Jin Zhan. 2004 Oct;35(4):306-10.


[Structure, function and modulation of actin-related protein 2/3 complex]

[Article in Chinese]

Gong XW, Jiang Y.

Department of Pathophysiology of the First Military Medical University.

Microfilaments, composed of global actins, involve in many important physiological activities, such as the maintenance of cell shape and cell migration. Actin-related protein 2/3 ( Arp2/3) complex plays a key role in microfilament formation. Actin-related protein 2/3 ( Arp2/3 ) complex which is composed of seven different subunits is subjected to the modulation of many nucleation promoting factors (NPFs) and cooperates with these factors to regulate the actin nucleation. The study of the structure, function and modulation of Arp2/3 complex is important in understanding the mechanism of the formation of microfilament and the interaction between cytoskeleton and signaling molecules.

Publication Types:
English Abstract
Research Support, Non-U.S. Gov't
Review

PMID: 15727206 [PubMed - indexed for MEDLINE]

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4: Results Probl Cell Differ. 2001;32:23-41.


Divalent cations, nucleotides, and actin structure.

Strzelecka-Gołaszewska H.

Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, 3 Pasteur Street, 02-093 Warsaw, Poland.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 11131834 [PubMed - indexed for MEDLINE]

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5: Results Probl Cell Differ. 2001;32:103-21.


Actin structure function relationships revealed by yeast molecular genetics.

Belmont LD, Drubin DG.

Department of Molecular and Cell Biology, 401 Barker Hall, University of California, Berkeley, California 94720-3202, USA.

Publication Types:
Review

PMID: 11131826 [PubMed - indexed for MEDLINE]

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6: Results Probl Cell Differ. 2001;32:1-7.


An overview of actin structure and actin-binding proteins.

dos Remedios CG, Thomas DD.

Institute for Biomedical Research, University of Sydney, Sydney 2006, Australia.

Publication Types:
Review

PMID: 11131825 [PubMed - indexed for MEDLINE]

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7: Seikagaku. 2000 May;72(5):388-92.


[Dynamic structure of muscle motor protein actin-myosin complex]

[Article in Japanese]

Arata T.

Department of Biology, Graduate School of Science, Osaka University.

Publication Types:
Review

PMID: 10879115 [PubMed - indexed for MEDLINE]

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8: Microsc Res Tech. 1999 Oct 1;47(1):38-50.


Structure, assembly, and dynamics of actin filaments in situ and in vitro.

Schoenenberger CA, Steinmetz MO, Stoffler D, Mandinova A, Aebi U.

M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, CH-4506 Basel, Switzerland. Schoenenberg@ubaclu.unibas.ch

Actin, though highly conserved, exhibits a myriad of diverse functions, most of which ultimately depend on its intrinsic ability to rapidly assemble and disassemble filamentous structures. Many organisms synthesize multiple actin isoforms even within the same cell. Tissue-specific expression patterns and tight developmental regulation as well as a high conservation across species emphasize the functional importance of isoforms. The detailed knowledge of the structure, assembly, and dynamic behavior of actin provides important pieces in solving the puzzle of how the different isoforms can be so versatile despite their extremely high sequence identity. Copyright 1999 Wiley-Liss, Inc.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 10506760 [PubMed - indexed for MEDLINE]

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9: Curr Opin Cell Biol. 1998 Feb;10(1):23-34.


The modular structure of actin-regulatory proteins.

Puius YA, Mahoney NM, Almo SC.

Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA.

Filamentous actin structures possess unique biophysical and biochemical properties and are required for cell locomotion, cell division, compartmentalization and morphological processes. The site-specific assembly and disassembly of these structures are directed by actin-regulatory proteins. This article reviews how structural studies are now defining the atomic details of small modular domains present in actin-regulatory proteins responsible for crosslinking, severing and capping of actin filaments, as well as for localization of actin filament assembly. These studies have identified three modular strategies for the design of proteins that regulate the actin cytoskeleton.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 9484592 [PubMed - indexed for MEDLINE]

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10: Int Rev Cytol. 1997;175:29-90.


The structure, function, and assembly of actin filament bundles.

Furukawa R, Fechheimer M.

Department of Cellular Biology, University of Georgia, Athens 30602, USA.

The cellular organization, function, and molecular composition of selected biological systems with prominent actin filament bundles are reviewed. An overall picture of the great variety of functions served by actin bundles emerges from this overview. A unifying theme is that the actin cross-linking proteins are conserved throughout the eukaryotic kingdom and yet assembled in a variety of combinations to produce actin bundles of differing functions. Mechanisms of actin bundle formation in vitro are considered illustrating the variety of physical and chemical driving forces in this exceedingly complex process. Our limited knowledge regarding the formation of actin filament bundles in vivo is contrasted with the elegant biophysical studies performed in vitro but nonetheless reveals that interactions with membranes, nucleation sites, and other organizational components must contribute to formation of actin bundles in vivo.

Publication Types:
Comparative Study
Research Support, U.S. Gov't, Non-P.H.S.
Review

PMID: 9203356 [PubMed - indexed for MEDLINE]

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11: Annu Rev Biophys Biomol Struct. 1996;25:137-62.


The sugar kinase/heat shock protein 70/actin superfamily: implications of conserved structure for mechanism.

Hurley JH.

Laboratory of Molecular Biology, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0580, USA.

Sugar kinases, stress-70 proteins, and actin belong to a superfamily defined by a fold consisting of two domains with the topology beta beta beta alpha beta alpha beta alpha. These enzymes catalyze ATP phosphoryl transfer or hydrolysis coupled to a large conformational change in which the two domains close around the nucleotide. The beta 1-beta 2 turns of each domain form hydrogen bonds with ATP phosphates, and conserved Asp, Glu or Gln residues coordinate Mg2+ or Ca2+ through bound waters. The activity of superfamily members is regulated by various effectors, some of which act by promoting or inhibiting the conformational change. Nucleotide hydrolysis eliminates interdomain bridging interactions between the second beta 1-beta 2 turn and the ATP gamma-phosphate. This is proposed to destabilize the closed conformation and affect the orientation of the two domains, which might in turn regulate the activity of kinase oligomers, stress-70 protein-protein complexes, and actin filaments.

Publication Types:
Review

PMID: 8800467 [PubMed - indexed for MEDLINE]

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12: Annu Rev Cell Biol. 1994;10:207-49.


Structure of actin binding proteins: insights about function at atomic resolution.

Pollard TD, Almo S, Quirk S, Vinson V, Lattman EE.

Department of Cell Biology and Anatomy, Johns Hopkins Medical School, Baltimore, Maryland 21205.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 7888177 [PubMed - indexed for MEDLINE]

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13: Tanpakushitsu Kakusan Koso. 1993 Mar;38(4):721-30.


[Structure and expression of actin genes]

[Article in Japanese]

Kusakabe T, Satoh N.

Department of Zoology, Faculty of Science, Kyoto University, Japan.

Publication Types:
English Abstract
Review

PMID: 8475328 [PubMed - indexed for MEDLINE]

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14: Curr Opin Cell Biol. 1993 Feb;5(1):41-7.


Actin molecular structure and function.

Reisler E.

Department of Chemistry and Biochemistry, University of California, Los Angeles 90024-1570.

The understanding of actin structure and function has been improved by comparing the atomic structure of G-actin, the model of the F-actin structure, and the properties of actin mutants. Several aspects of actin structure have been tested and good progress has been made in mapping its myosin-binding sites. The dynamic properties of actin and genetic evaluation of its cellular function are attracting increasing attention.

Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 8448029 [PubMed - indexed for MEDLINE]

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15: J Muscle Res Cell Motil. 1992 Apr;13(2):132-45.


Structure of actin observed by fluorescence resonance energy transfer spectroscopy.

Miki M, O'Donoghue SI, Dos Remedios CG.

Department of Anatomy, University of Sydney, Australia.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 1534564 [PubMed - indexed for MEDLINE]

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16: Curr Opin Cell Biol. 1992 Feb;4(1):20-6.


The structure of the F-actin filament and the actin molecule.

Bremer A, Aebi U.

ME Müller-Institute for High-Resolution Electron Microscopy at the Biocenter, University of Basel, Basel, Switzerland.

A consensus view on the three-dimensional structure of the F-actin filament and the relative strength of the intersubunit contacts in the filament has been established from an atomic filament model and recent three-dimensional reconstructions from electron micrographs of F-actin filaments. Functional implications of recent structural and biochemical data indicating a rather dynamic filament structure are discussed.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 1558750 [PubMed - indexed for MEDLINE]

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17: Annu Rev Biophys Biomol Struct. 1992;21:49-76.


Structure and function of actin.

Kabsch W, Vandekerckhove J.

Max-Planck-Institut für medizinische Forschung, Abteilung Biophysik, Heidelberg, Germany.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 1388079 [PubMed - indexed for MEDLINE]

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18: Bioessays. 1991 May;13(5):219-26.


Structure and evolution of the actin crosslinking proteins.

Dubreuil RR.

Biological Laboratories, Harvard University, Cambridge, MA 02138.

The actin crosslinking proteins exhibit marked diversity in size and shape and crosslink actin filaments in different ways. Amino acid sequence analysis of many of these proteins has provided clues to the origin of their diversity. Spectrin, alpha-actinin, ABP-120, ABP-280, fimbrin, and dystrophin share a homologous sequence segment that is implicated as the common actin binding domain. The remainder of each protein consists of repetitive and non-repetitive sequence segments that have been shuffled and multiplied in evolution to produce a variety of proteins that are related in function and in composition, but that differ significantly in structure.

Publication Types:
Comparative Study
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 1892474 [PubMed - indexed for MEDLINE]

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19: J Biol Chem. 1991 Jan 5;266(1):1-4.


Actin: protein structure and filament dynamics.

Carlier MF.

Laboratoire d'Enzymologie, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France.

Publication Types:
Review

PMID: 1985885 [PubMed - indexed for MEDLINE]

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20: Bioessays. 1990 Sep;12(9):403-8.


From the structure to the function of villin, an actin-binding protein of the brush border.

Friederich E, Pringault E, Arpin M, Louvard D.

Département de Biologie Moléculaire, Institut Pasteur, Paris.

Villin, a calcium-regulated actin-binding protein, modulates the structure and assembly of actin filaments in vitro. It is organized into three domains, the first two of which are homologous. Villin is mainly produced in epithelial cells that develop a brush border and which are responsible for nutrient uptake. Expression of the villin structural gene is precisely regulated during mouse embryogenesis and is restricted in adults, to certain epithelia of the gastrointestinal and urogenital tracts. The function of villin has been assessed by transfecting CV1 cells with a human cDNA encoding wild-type villin or mutant villin. Synthesis of large amounts of villin in cells which do not normally produce this protein induces the growth of microvilli on the cell surface and the redistribution of F-actin, concomitant with the disappearance of stress fibers. The complete villin sequence is required for the morphogenic effect. These results suggest that villin plays a key role in the morphogenesis of microvilli.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 2256904 [PubMed - indexed for MEDLINE]

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21: Eur J Surg Oncol. 1990 Apr;16(2):161-9.


Cancer cell structure: actin changes in tumour cells--possible mechanisms for malignant tumour formation.

Holme TC.

Ninewells Hospital, Dundee, Scotland.

Improvement in treatment of solid tumours is likely to depend on a better knowledge of the biological mechanisms of malignant tumour formation. Over the past few years a great deal of progress has occurred in our understanding of cell biology, and one of the main areas of development has been the cell cytoskeleton. The cytoskeleton contributes to maintenance of cell structure and to a variety of other cell functions. Several studies have implicated one of the elements of the cytoskeleton, the microfilaments, in malignant change, and these microfilaments are directly affected by the activity of some 'oncogenes'. Changes in the control of filament polymerization and organization have been demonstrated in response to the activity of the src oncogene. The protease trypsin has been shown to affect the actin cytoskeleton grossly and illustrates that proteases released in the vicinity of tumours may have a biologically significant effect on the internal structure and stability of the cell. Further investigation of the microfilament system may reveal important clues for future manipulation of the cancer cell and the treatment of the patient with advanced cancer.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 2182342 [PubMed - indexed for MEDLINE]

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22: Cell Motil Cytoskeleton. 1989;14(1):35-9.


Actin structure-function relationships in vitro using oligodeoxynucleotide-directed site-specific mutagenesis.

Rubenstein PA, Solomon LR, Solomon T, Gay L.

Department of Biochemistry, University of Iowa College of Medicine, Iowa City 52242.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2684425 [PubMed - indexed for MEDLINE]

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23: Adv Exp Med Biol. 1989;255:315-23.


Calcium and polyphosphoinositide regulation of actin network structure by gelsolin.

Yin HL.

Hematology-Oncology Unit, Massachusetts General Hospital, Harvard Medical School, Boston 02114.

Publication Types:
Review

PMID: 2559597 [PubMed - indexed for MEDLINE]

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24: J Cell Sci Suppl. 1988;9:169-84.


The structure of the macrophage actin skeleton.

Yin HL, Hartwig JH.

Hematology-Oncology Unit, Massachusetts General Hospital and Harvard Medical School, Boston.

The actin skeleton of the macrophage consists of a three-dimensional network of actin filaments and associated proteins. The organization of this multiprotein structure is regulated at several levels in cells. Receptor stimulation induces a massive actin polymerization at the cell cortex, changes in cell shape and active cellular movements. Gelsolin may have a pivotal role in restructuring the actin skeleton in response to agonist stimulation, as the activity of this potent actin-modulating protein is regulated by both Ca2+ and polyphosphoinositides. Micromolar concentrations of Ca2+ activate gelsolin to bind to the sides of actin filaments, sever, and cap the filament end. Polyphosphoinositides, in particular PIP and PIP2, release gelsolin from the filament ends. A structure-function analysis of gelsolin indicates that its N-terminal half is primarily responsible for severing actin filaments, and elucidates mechanisms by which Ca2+ and phospholipid may regulate gelsolin functions. The ultrastructure of actin filaments in the macrophage cortical cytoplasm is regulated, to a large extent, by the actin cross-linking protein, actin-binding protein (ABP) which defines filament orthogonality.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2855803 [PubMed - indexed for MEDLINE]

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25: J Muscle Res Cell Motil. 1985 Apr;6(2):129-51.


The structure of F-actin.

Egelman EH.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 3897278 [PubMed - indexed for MEDLINE]

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26: J Cell Biol. 1984 Jul;99(1 Pt 2):15s-21s.


Contribution of actin to the structure of the cytoplasmic matrix.

Stossel TP.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 6086665 [PubMed - indexed for MEDLINE]

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27: Cold Spring Harb Symp Quant Biol. 1982;46 Pt 2:569-78.


Actin gelation and structure of cortical cytoplasm.

Stossel TP, Hartwig JH, Yin HL, Zaner KS, Stendahl OI.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 6286216 [PubMed - indexed for MEDLINE]

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28: J Histochem Cytochem. 1975 Jul;23(7):507-28.


Immunofluorescence studies on the structure of actin filaments in tissue culture cells.

Lazarides E.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 1095651 [PubMed - indexed for MEDLINE]

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29: Seikagaku. 1967 Jun 25;39(6):322-31.


[Beta-actinin--structure regulating factor of F-actin]

[Article in Japanese]

Maruyama K.

Publication Types:
Review

PMID: 4864955 [PubMed - indexed for MEDLINE]
 

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