| pubmed-article:9480911 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9480911 | lifeskim:mentions | umls-concept:C1334088 | lld:lifeskim |
| pubmed-article:9480911 | lifeskim:mentions | umls-concept:C0140080 | lld:lifeskim |
| pubmed-article:9480911 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9480911 | lifeskim:mentions | umls-concept:C0033713 | lld:lifeskim |
| pubmed-article:9480911 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:9480911 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:9480911 | pubmed:dateCreated | 1998-4-16 | lld:pubmed |
| pubmed-article:9480911 | pubmed:abstractText | The Crk proto-oncogene product is an SH2 and SH3 domain-containing adaptor protein. We have previously demonstrated that Crk-II becomes rapidly tyrosine-phosphorylated in response to stimulation with insulin-like growth factor I (IGF-I) and might be involved in the IGF-I receptor signalling pathway. To determine whether this involvement includes the direct interaction of Crk-II with the cytoplasmic region of the receptor, studies were performed in vitro with glutathione S-transferase (GST) fusion proteins containing various domains of Crk-II. The kinase assay in vitro showed that activated IGF-I receptors efficiently phosphorylated the GST-Crk-II fusion protein. This phosphorylation was dependent on the presence of the SH2 domain and Tyr-221 located in the spacer region between the two SH3 domains. Mutation of Tyr-221 not only prevented phosphorylation of GST-Crk in vitro, but also significantly increased the ability of GST-Crk proteins to co-precipitate activated IGF-I receptors from total cell lysates. Additional binding experiments in vitro showed that Crk-II might interact with the phosphorylated IGF-I receptor through its SH2 domain. To elucidate which region of the IGF-I receptor interacts with Crk-II, a peptide association assay was used in vitro. Different domains of the IGF-I receptor were expressed as (His)6-tagged fusion peptides, phosphorylated with activated wheat germ agglutinin-purified IGF-I receptors and tested for association with GST-Crk-II fusion proteins. Using wild-type as well as mutated peptides, we showed that the SH2 domain of Crk-II preferentially binds the peptide encoding the juxtamembrane region of the IGF-I receptor. Phosphorylation of Tyr-950 and Tyr-943 of the receptor is important for this interaction. These findings allow us to propose a model of direct interaction of Crk-II and the IGF-I receptor in vivo. On activation of the IGF-I receptor, Crk-II binds to phosphorylated tyrosine residues, especially in the juxtamembrane region. As a result of this binding, the IGF-I receptor kinase phosphorylates Tyr-221 of Crk-II, resulting in a change in intramolecular folding and binding of the SH2 domain to the phosphorylated Tyr-221, which causes rapid disassociation of the Crk-II-IGF-I receptor complex. | lld:pubmed |
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| pubmed-article:9480911 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9480911 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9480911 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9480911 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9480911 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9480911 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9480911 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:9480911 | pubmed:author | pubmed-author:ZickYY | lld:pubmed |
| pubmed-article:9480911 | pubmed:author | pubmed-author:LeroithDD | lld:pubmed |
| pubmed-article:9480911 | pubmed:author | pubmed-author:RobertsC... | lld:pubmed |
| pubmed-article:9480911 | pubmed:author | pubmed-author:KovalA PAP | lld:pubmed |
| pubmed-article:9480911 | pubmed:author | pubmed-author:BlakesleyV... | lld:pubmed |
| pubmed-article:9480911 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9480911 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9480911 | pubmed:volume | 330 ( Pt 2) | lld:pubmed |
| pubmed-article:9480911 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9480911 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9480911 | pubmed:pagination | 923-32 | lld:pubmed |
| pubmed-article:9480911 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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