Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation.

Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation. Research Abstract Details 

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Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation. Abstract Text:

Gabriel Gaidos,Shefali Soni,Duane J Oswald,Paul A Toselli,Kathrin H Kirsch,

Members of the CMS/CIN85 protein family participate in clathrin-mediated endocytosis and play a crucial role in maintaining the kidney filtration barrier. The CMS protein structure includes three Src homology 3 (SH3) domains and a proline-rich (PR) region that is connected by a 'linker' sequence to a coiled-coil (CC) domain. We show that CMS is a component of special actin-rich adhesion structures--podosomes--and demonstrate specific actin-binding properties of CMS. We have found that the entire C-terminal half of CMS is necessary for efficient binding to filamentous actin (F-actin). CMS and CIN85 can crosslink F-actin into bundles, a function that depends on the PR region and the CC domain. Removal of these domains reduces migration. CMS can also form heterotypic complexes with CIN85. CIN85 is expressed as multiple isoforms that share the CC domain, suggesting that heterotypic interactions with CMS provides a mechanism to regulate CMS binding to F-actin and thus for modulating dynamic rearrangements of the cytoskeleton.

Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation. Publishing Authors By Initials

G Gaidos,S Soni,DJ Oswald,PA Toselli,KH Kirsch,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation: protein structure, tertiary: protein interaction domains and motifs: src homology domains research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation: protein structure, tertiary: protein interaction domains and motifs: src homology domains research

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Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of cell science

VOLUME: 120

Page Numbers: 2366-77

Journal Abbreviation: J. Cell. Sci.

ISSN: 0021-9533

DAY: 15

MONTH: Jul

YEAR: 2007

Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 52457

Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation. Keywords Mesh Terms:

KEYWORDS: src Homology Domains

MESH TERMS: physiology

Chemical & Substance for Abstract: Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation. Information

Substance Name: SH3KBP1 protein, human

Registry Number: 0

Grant and Affiliation Information for Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation.

AFFILIATION: Department of Biochemistry, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118, USA.

Country: England

AGENCY: United States NCI

GRANT: CA106468

ACRONYM: CA

MEDLINETA: J Cell Sci

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