Source:http://linkedlifedata.com/resource/pubmed/id/17020880
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
50
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pubmed:dateCreated |
2006-12-12
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pubmed:databankReference | |
pubmed:abstractText |
The CIN85/CMS (human homologs of mouse SH3KBP1/CD2AP) family of endocytic adaptor proteins has the ability to engage multiple effectors and couple cargo trafficking with the cytoskeleton. CIN85 and CMS (Cas ligand with multiple Src homology 3 (SH3) domains) facilitate the formation of large multiprotein complexes required for an efficient internalization of cell surface receptors. It has recently been shown that c-Cbl/Cbl-b could mediate the formation of a ternary complex between one c-Cbl/Cbl-b molecule and two SH3 domains of CIN85, important for the ability of Cbl to promote epidermal growth factor receptor down-regulation. To further investigate whether multimerization is conserved within the family of adaptor proteins, we have solved the crystal structures of the CMS N-terminal SH3 domain-forming complexes with Cbl-b- and CD2-derived peptides. Together with biochemical evidence, the structures support the notion that, despite clear differences in the interaction surface, both Cbl-b and CD2 can mediate multimerization of N-terminal CMS SH3 domains. Detailed analyses on the interacting surfaces also provide the basis for a differential Cbl-b molecular recognition of CMS and CIN85.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/CD2-associated protein,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/polyproline
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
38845-53
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pubmed:meshHeading |
pubmed-meshheading:17020880-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:17020880-Amino Acid Sequence,
pubmed-meshheading:17020880-Binding Sites,
pubmed-meshheading:17020880-Crystallography, X-Ray,
pubmed-meshheading:17020880-Cytoskeletal Proteins,
pubmed-meshheading:17020880-Humans,
pubmed-meshheading:17020880-Models, Molecular,
pubmed-meshheading:17020880-Molecular Sequence Data,
pubmed-meshheading:17020880-Peptides,
pubmed-meshheading:17020880-Protein Conformation,
pubmed-meshheading:17020880-Sequence Homology, Amino Acid,
pubmed-meshheading:17020880-src Homology Domains
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pubmed:year |
2006
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pubmed:articleTitle |
Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain.
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pubmed:affiliation |
Signal Transduction Group, Structural Biology and Biocomputing Programme, Centro Nacional de Investigaciones Oncológicas, Melchor Fernández Almagro 3, E-28029 Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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