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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2004-11-3
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pubmed:abstractText |
The SH2/SH3 adapter proteins of the Crk family are potent signal transducers after receptor tyrosine kinase stimulation with insulin or IGF-1. We have employed a yeast two-hybrid approach and mutational analysis to dissect the capabilities of the insulin receptor and the IGF-I receptor to directly associate with Crk isoforms. Insulin receptor stably recruits full length Crk by association with its SH2 domain in an auto-phosphorylation dependent manner. In contrast, interaction of the IGF-I receptor with the Crk-IISH2 domain was only detectable when Crk-II was truncated in its C-terminal part, indicating the transient nature of this interaction. From these data it can be concluded that members of the insulin receptor family activate Crk proteins in a differential manner.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/CRKL protein,
http://linkedlifedata.com/resource/pubmed/chemical/NIMA-interacting peptidylprolyl...,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidylprolyl Isomerase,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
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/Receptor, IGF Type 1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
325
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
183-90
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15522217-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:15522217-Cell Line,
pubmed-meshheading:15522217-DNA Mutational Analysis,
pubmed-meshheading:15522217-Humans,
pubmed-meshheading:15522217-Nuclear Proteins,
pubmed-meshheading:15522217-Peptidylprolyl Isomerase,
pubmed-meshheading:15522217-Protein Isoforms,
pubmed-meshheading:15522217-Proto-Oncogene Proteins,
pubmed-meshheading:15522217-Proto-Oncogene Proteins c-crk,
pubmed-meshheading:15522217-Receptor, IGF Type 1,
pubmed-meshheading:15522217-Receptor, Insulin,
pubmed-meshheading:15522217-Recombinant Fusion Proteins,
pubmed-meshheading:15522217-Two-Hybrid System Techniques,
pubmed-meshheading:15522217-src Homology Domains
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pubmed:year |
2004
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pubmed:articleTitle |
Mutational analysis of the interaction between insulin receptor and IGF-I receptor with c-Crk and Crk-L in a yeast two-hybrid system.
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pubmed:affiliation |
Hospital for Children and Adolescents, University of Leipzig, 04317 Leipzig, Oststrasse 21-25, Germany. juergen.klammt@medzin.uni-leipzig.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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