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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2-3
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pubmed:dateCreated |
2002-10-9
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pubmed:abstractText |
The vasodilator-stimulated phosphoprotein (VASP) functions as a cellular regulator of actin dynamics. VASP may initialise actin polymerisation, suggesting a direct interaction with monomeric actin. The present study demonstrates that VASP directly binds to actin monomers and that complex formation depends on a conserved four amino acid motif in the EVH2 domain. Point mutations within this motif drastically weaken VASP/G-actin interactions, thereby abolishing any actin-nucleating activity of VASP. Additionally, actin nucleation was found to depend on VASP oligomerisation since VASP monomers fail to induce the formation of actin filaments. Phosphorylation negatively affects VASP/G-actin interactions preventing VASP-induced actin filament formation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
529
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
275-80
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12372613-Actins,
pubmed-meshheading:12372613-Amino Acid Motifs,
pubmed-meshheading:12372613-Amino Acid Sequence,
pubmed-meshheading:12372613-Animals,
pubmed-meshheading:12372613-Biopolymers,
pubmed-meshheading:12372613-Cell Adhesion Molecules,
pubmed-meshheading:12372613-Contractile Proteins,
pubmed-meshheading:12372613-Mice,
pubmed-meshheading:12372613-Microfilament Proteins,
pubmed-meshheading:12372613-Molecular Sequence Data,
pubmed-meshheading:12372613-Phosphoproteins,
pubmed-meshheading:12372613-Phosphorylation,
pubmed-meshheading:12372613-Point Mutation,
pubmed-meshheading:12372613-Profilins,
pubmed-meshheading:12372613-Protein Binding,
pubmed-meshheading:12372613-Sequence Homology, Amino Acid
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pubmed:year |
2002
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pubmed:articleTitle |
The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin.
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pubmed:affiliation |
Cell Biology, Zoological Institute, Technical University of Braunschweig, Biocenter, Spielmannstrasse 7, D-38092 Braunschweig, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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