rdf:type |
|
lifeskim:mentions |
|
pubmed:dateCreated |
1998-5-21
|
pubmed:abstractText |
Cell adhesion kinase beta (CAKbeta) is a protein tyrosine kinase closely related to focal adhesion kinase (FAK) in structure. CAKbeta contains two proline-rich sequences within its C-terminal region. Since proline-rich sequences present in the corresponding region of FAK are known to mediate protein-protein interactions by binding to SH3 domains, we investigated binding of CAKbeta to a panel of SH3 domains. Affinity precipitation from rat brain lysate revealed selective interactions of CAKbeta with glutathione S-transferase (GST)-fused SH3 domains of p130(Cas)(Cas)-related proteins and Graf. Mutational analysis indicated that the proline-rich sequences of CAKbeta mediate this interaction. Each of the two proline-rich sequences fused to GST bound directly to these SH3 domains in dot blot analysis. A competitive binding assay revealed that the first proline-rich sequence of CAKbeta preferentially associated with the SH3 domain of Cas. The second proline-rich sequence of CAKbeta bound to the SH3 domain of Graf with higher specificity than the corresponding proline-rich sequence of FAK. Finally, we showed co-immunoprecipitation of CAKbeta with Graf from rat brain lysate. These results indicate that CAKbeta associates in vivo with Graf through its SH3 domain.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-1630456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-2828856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-3162824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-3185726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7479864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7499242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7505391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7510218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7526465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7531822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7537275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7544443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7561682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7673154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7685110,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7802869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7834743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7938008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-7997267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8070403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8334708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8402898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8526861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8570184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8585605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8596638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8606775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8618911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8649427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8662921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8668148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8670418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8681387,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8687411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8761480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8849729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8887669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8910543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8940124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8940134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-8995252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-9020138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-9104812,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-9148966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-9312150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-9349509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9494093-9422762
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bcar1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Crk-Associated Substrate Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ptk2b protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma-Like Protein p130
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0264-6021
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
330 ( Pt 3)
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1249-54
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:9494093-Animals,
pubmed-meshheading:9494093-Proteins,
pubmed-meshheading:9494093-Brain,
pubmed-meshheading:9494093-Rats,
pubmed-meshheading:9494093-Proline,
pubmed-meshheading:9494093-Kinetics,
pubmed-meshheading:9494093-Amino Acid Sequence,
pubmed-meshheading:9494093-Binding Sites,
pubmed-meshheading:9494093-Phosphoproteins,
pubmed-meshheading:9494093-Sequence Alignment,
pubmed-meshheading:9494093-Sequence Homology, Amino Acid,
pubmed-meshheading:9494093-Glutathione Transferase,
pubmed-meshheading:9494093-Transfection,
pubmed-meshheading:9494093-Protein-Tyrosine Kinases
|