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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
40
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pubmed:dateCreated |
1998-11-12
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pubmed:abstractText |
p130(Cas) (Cas; crk-associated substrate) belongs to a new family of docking molecules. It contains one Src homology (SH) 3 domain in its amino-terminal region followed by a region containing binding motifs for SH2 and SH3 domains. To gain further insight into Cas signaling we used the SH3 domain of Cas in a two-hybrid screen to search a human placenta library for binding partners. The screen confirmed a previous finding of its binding to the focal adhesion kinase (FAK) but also identified C3G, a guanine nucleotide exchange factor. We found direct interaction between Cas and C3G in vitro and in vivo. A series of analysis with C3G deletion mutants revealed a proline-rich Cas-binding site (Ala0-Pro1-Pro2-Lys3-Pro4-Pro5-Leu6-Pro7) located NH2-terminal to the previously characterized Crk binding motifs in C3G. Mutagenesis studies showed that Pro1, Lys3, and Pro4 within the ligand-binding site are critical for high affinity interaction. These results, combined with sequence alignments of proline-rich binding elements from proteins known for Cas binding, define the consensus sequence XXPXKPX which is recognized by the CasSH3 domain. Cas shows structural characteristics of a docking molecule and may serve to bring C3G to specific compartments within the cell.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/BCAR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Crk-Associated Substrate Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-crk,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma-Like Protein p130
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25673-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9748234-Amino Acid Sequence,
pubmed-meshheading:9748234-Binding Sites,
pubmed-meshheading:9748234-Consensus Sequence,
pubmed-meshheading:9748234-Crk-Associated Substrate Protein,
pubmed-meshheading:9748234-DNA Mutational Analysis,
pubmed-meshheading:9748234-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:9748234-Humans,
pubmed-meshheading:9748234-Molecular Sequence Data,
pubmed-meshheading:9748234-Mutagenesis, Site-Directed,
pubmed-meshheading:9748234-Phosphoproteins,
pubmed-meshheading:9748234-Placenta,
pubmed-meshheading:9748234-Proline,
pubmed-meshheading:9748234-Protein Binding,
pubmed-meshheading:9748234-Proteins,
pubmed-meshheading:9748234-Proto-Oncogene Proteins,
pubmed-meshheading:9748234-Proto-Oncogene Proteins c-crk,
pubmed-meshheading:9748234-Recombinant Fusion Proteins,
pubmed-meshheading:9748234-Retinoblastoma-Like Protein p130,
pubmed-meshheading:9748234-Sequence Alignment,
pubmed-meshheading:9748234-Sequence Deletion,
pubmed-meshheading:9748234-src Homology Domains
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pubmed:year |
1998
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pubmed:articleTitle |
Direct binding of p130(Cas) to the guanine nucleotide exchange factor C3G.
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pubmed:affiliation |
Laboratory of Molecular Oncology, The Rockefeller University, New York, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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