Intermediate Filament Interactions
Published by Anonymous on 2007/9/28 (2864 reads)
1: Braz J Med Biol Res. 2004 Dec;37(12):1819-30. Epub 2004 Nov 17.
Desmin: molecular interactions and putative functions of the muscle intermediate filament protein.
Costa ML, Escaleira R, Cataldo A, Oliveira F, Mermelstein CS.
Laboratório de Diferenciação Muscular e Citoesqueleto, Departamento de Histologia e Embriologia, Instituto de Ciências Biomédicas, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil. manoelluiscosta@ufrj.br
Desmin is the intermediate filament (IF) protein occurring exclusively in muscle and endothelial cells. There are other IF proteins in muscle such as nestin, peripherin, and vimentin, besides the ubiquitous lamins, but they are not unique to muscle. Desmin was purified in 1977, the desmin gene was characterized in 1989, and knock-out animals were generated in 1996. Several isoforms have been described. Desmin IFs are present throughout smooth, cardiac and skeletal muscle cells, but can be more concentrated in some particular structures, such as dense bodies, around the nuclei, around the Z-line or in costameres. Desmin is up-regulated in muscle-derived cellular adaptations, including conductive fibers in the heart, electric organs, some myopathies, and experimental treatments with drugs that induce muscle degeneration, like phorbol esters. Many molecules have been reported to associate with desmin, such as other IF proteins (including members of the membrane dystroglycan complex), nebulin, the actin and tubulin binding protein plectin, the molecular motor dynein, the gene regulatory protein MyoD, DNA, the chaperone alphaB-crystallin, and proteases such as calpain and caspase. Desmin has an important medical role, since it is used as a marker of tumors' origin. More recently, several myopathies have been described, with accumulation of desmin deposits. Yet, after almost 30 years since its identification, the function of desmin is still unclear. Suggested functions include myofibrillogenesis, mechanical support for the muscle, mitochondrial localization, gene expression regulation, and intracellular signaling. This review focuses on the biochemical interactions of desmin, with a discussion of its putative functions.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 15558188 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: 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]
--------------------------------------------------------------------------------
3: Curr Opin Struct Biol. 1998 Apr;8(2):177-85.
Intermediate filament assembly: fibrillogenesis is driven by decisive dimer-dimer interactions.
Herrmann H, Aebi U.
Division of Cell Biology, German Cancer Research Center, Heidelberg, Germany. H.Herrmann@DKFZ-Heidelberg.de
Intermediate filaments are built from one to several members of a multigene family encoding fibrous proteins that share a highly conserved hierarchic assembly plan for the formation of multistranded filaments from distinctly structured extended coiled coils. Despite the rather low primary sequence identity, intermediate filaments form apparently similar filaments with regard to their spatial dimensions and physical properties. Over the past few years, substantial progress has been made in the elucidation of the complex expression patterns and clinically relevant phenotypes of intermediate filaments. The key question of how these filaments assemble and what the molecular architecture of their distinct assembly intermediates comprises, however, has still not been answered to the extent that has been achieved for microfilaments and microtubules.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9631290 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Curr Opin Cell Biol. 1991 Feb;3(1):127-32.
Intermediate filament-plasma membrane interactions.
Jones JC, Green KJ.
Department of Cell, Molecular and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611.
In this review we will discuss the molecules involved in intermediate filament-desmosome and intermediate filament-hemidesmosome interactions, and the means by which certain of these molecules may bind to intermediate filaments. The possibility that intermediate filaments interact directly with peripheral membrane proteins and membrane lipids will also be addressed.
Publication Types:
Review
PMID: 1854477 [PubMed - indexed for MEDLINE]
Desmin: molecular interactions and putative functions of the muscle intermediate filament protein.
Costa ML, Escaleira R, Cataldo A, Oliveira F, Mermelstein CS.
Laboratório de Diferenciação Muscular e Citoesqueleto, Departamento de Histologia e Embriologia, Instituto de Ciências Biomédicas, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil. manoelluiscosta@ufrj.br
Desmin is the intermediate filament (IF) protein occurring exclusively in muscle and endothelial cells. There are other IF proteins in muscle such as nestin, peripherin, and vimentin, besides the ubiquitous lamins, but they are not unique to muscle. Desmin was purified in 1977, the desmin gene was characterized in 1989, and knock-out animals were generated in 1996. Several isoforms have been described. Desmin IFs are present throughout smooth, cardiac and skeletal muscle cells, but can be more concentrated in some particular structures, such as dense bodies, around the nuclei, around the Z-line or in costameres. Desmin is up-regulated in muscle-derived cellular adaptations, including conductive fibers in the heart, electric organs, some myopathies, and experimental treatments with drugs that induce muscle degeneration, like phorbol esters. Many molecules have been reported to associate with desmin, such as other IF proteins (including members of the membrane dystroglycan complex), nebulin, the actin and tubulin binding protein plectin, the molecular motor dynein, the gene regulatory protein MyoD, DNA, the chaperone alphaB-crystallin, and proteases such as calpain and caspase. Desmin has an important medical role, since it is used as a marker of tumors' origin. More recently, several myopathies have been described, with accumulation of desmin deposits. Yet, after almost 30 years since its identification, the function of desmin is still unclear. Suggested functions include myofibrillogenesis, mechanical support for the muscle, mitochondrial localization, gene expression regulation, and intracellular signaling. This review focuses on the biochemical interactions of desmin, with a discussion of its putative functions.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 15558188 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: 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]
--------------------------------------------------------------------------------
3: Curr Opin Struct Biol. 1998 Apr;8(2):177-85.
Intermediate filament assembly: fibrillogenesis is driven by decisive dimer-dimer interactions.
Herrmann H, Aebi U.
Division of Cell Biology, German Cancer Research Center, Heidelberg, Germany. H.Herrmann@DKFZ-Heidelberg.de
Intermediate filaments are built from one to several members of a multigene family encoding fibrous proteins that share a highly conserved hierarchic assembly plan for the formation of multistranded filaments from distinctly structured extended coiled coils. Despite the rather low primary sequence identity, intermediate filaments form apparently similar filaments with regard to their spatial dimensions and physical properties. Over the past few years, substantial progress has been made in the elucidation of the complex expression patterns and clinically relevant phenotypes of intermediate filaments. The key question of how these filaments assemble and what the molecular architecture of their distinct assembly intermediates comprises, however, has still not been answered to the extent that has been achieved for microfilaments and microtubules.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9631290 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Curr Opin Cell Biol. 1991 Feb;3(1):127-32.
Intermediate filament-plasma membrane interactions.
Jones JC, Green KJ.
Department of Cell, Molecular and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611.
In this review we will discuss the molecules involved in intermediate filament-desmosome and intermediate filament-hemidesmosome interactions, and the means by which certain of these molecules may bind to intermediate filaments. The possibility that intermediate filaments interact directly with peripheral membrane proteins and membrane lipids will also be addressed.
Publication Types:
Review
PMID: 1854477 [PubMed - indexed for MEDLINE]
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