Source:http://linkedlifedata.com/resource/pubmed/id/16157603
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
45
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pubmed:dateCreated |
2005-11-7
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pubmed:abstractText |
HS1 (hematopoietic lineage cell-specific protein 1), a substrate of protein tyrosine kinases in lymphocytes, binds to F-actin, and promotes Arp2/3 complex-mediated actin polymerization. However, the mechanism for the interaction between HS1 and F-actin has not yet been fully characterized. HS1 contains 3.5 tandem repeats, a coiled-coil region, and an SH3 domain at the C terminus. Unlike cortactin, which is closely related to HS1 and requires absolutely the repeat domain for F-actin binding, an HS1 mutant with deletion of the repeat domain maintains a significant F-actin binding activity. On the other hand, deletion of the coiled-coil region abolished the ability of HS1 to bind to actin filaments and to activate the Arp2/3 complex for actin nucleation and actin branching. Furthermore, a peptide containing the coiled-coil sequence only was sufficient for F-actin binding. Within cells overexpressing green fluorescent protein-tagged HS1 proteins, wild type HS1 co-localizes with cortical F-actin at the cell leading edge, whereas mutants with deletion of either the coiled-coil region or the repeat domain diffuse in the cytoplasm. Immunoprecipitation analysis reveals that the coiled-coil deletion mutant binds poorly to F-actin, whereas the mutant without the repeat domain fails to bind to both Arp2/3 complex and F-actin. These data suggest that the HS1 coiled-coil region acts synergistically with the repeat domain in the modulation of the Arp2/3 complex-mediated actin polymerization.
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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/Actin-Related Protein 2-3 Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/HAX1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
37988-94
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16157603-Actin-Related Protein 2-3 Complex,
pubmed-meshheading:16157603-Actins,
pubmed-meshheading:16157603-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:16157603-Amino Acid Motifs,
pubmed-meshheading:16157603-Animals,
pubmed-meshheading:16157603-Cells, Cultured,
pubmed-meshheading:16157603-Endothelial Cells,
pubmed-meshheading:16157603-Humans,
pubmed-meshheading:16157603-Mutation,
pubmed-meshheading:16157603-Protein Binding,
pubmed-meshheading:16157603-Protein Structure, Tertiary,
pubmed-meshheading:16157603-Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
The coiled-coil domain is required for HS1 to bind to F-actin and activate Arp2/3 complex.
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pubmed:affiliation |
Department of Pathology, Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, 20855, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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