Source:http://linkedlifedata.com/resource/pubmed/id/17376963
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 7
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pubmed:dateCreated |
2007-3-22
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pubmed:abstractText |
Profilin and cyclase-associated protein (CAP, known in yeast as Srv2) are ubiquitous and abundant actin monomer-binding proteins. Profilin catalyses the nucleotide exchange on actin monomers and promotes their addition to filament barbed ends. Srv2/CAP recycles newly depolymerized actin monomers from ADF/cofilin for subsequent rounds of polymerization. Srv2/CAP also harbors two proline-rich motifs and has been suggested to interact with profilin. However, the mechanism and biological role of the possible profilin-Srv2/CAP interaction has not been investigated. Here, we show that Saccharomyces cerevisiae Srv2 and profilin interact directly (K(D) approximately 1.3 microM) and demonstrate that a specific proline-rich motif in Srv2 mediates this interaction in vitro and in vivo. ADP-actin monomers and profilin do not interfere with each other's binding to Srv2, suggesting that these three proteins can form a ternary complex. Genetic and cell biological analyses on an Srv2 allele (srv2-201) defective in binding profilin reveals that a direct interaction with profilin is not essential for Srv2 cellular function. However, srv2-201 causes a moderate increase in cell size and partially suppresses the cell growth and actin organization defects of an actin binding mutant profilin (pfy1-4). Together these data suggest that Srv2 is an important physiological interaction partner of profilin.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Profilins,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/SRV2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
120
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1225-34
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17376963-Actins,
pubmed-meshheading:17376963-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:17376963-Alleles,
pubmed-meshheading:17376963-Amino Acid Motifs,
pubmed-meshheading:17376963-Amino Acid Sequence,
pubmed-meshheading:17376963-Cell Cycle Proteins,
pubmed-meshheading:17376963-Cell Size,
pubmed-meshheading:17376963-Cytoskeletal Proteins,
pubmed-meshheading:17376963-Immunoprecipitation,
pubmed-meshheading:17376963-Kinetics,
pubmed-meshheading:17376963-Mutation,
pubmed-meshheading:17376963-Profilins,
pubmed-meshheading:17376963-Proline,
pubmed-meshheading:17376963-Protein Binding,
pubmed-meshheading:17376963-Saccharomyces cerevisiae,
pubmed-meshheading:17376963-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:17376963-Spectrometry, Fluorescence
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pubmed:year |
2007
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pubmed:articleTitle |
Mechanism and biological role of profilin-Srv2/CAP interaction.
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pubmed:affiliation |
Institute of Biotechnology, University of Helsinki, 00014 Helsinki, Finland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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