| pubmed-article:7537849 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C0034818 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C1334140 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C0123658 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C1312062 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C1705297 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:7537849 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:7537849 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:7537849 | pubmed:dateCreated | 1995-6-2 | lld:pubmed |
| pubmed-article:7537849 | pubmed:abstractText | The SHC proteins have been implicated in insulin receptor (IR) signaling. In this study, we used the sensitive two-hybrid assay of protein-protein interaction to demonstrate that SHC interacts directly with the IR. The interaction is mediated by SHC amino acids 1 to 238 and is therefore independent of the Src homology 2 domain. The interaction is dependent upon IR autophosphorylation, since the interaction is eliminated by mutation of the IR ATP-binding site. In addition, mutational analysis of the Asn-Pro-Glu-Tyr (NPEY) motif within the juxtamembrane domain of the IR showed the importance of the Asn, Pro, and Tyr residues to both SHC and IR substrate 1 (IRS-1) binding. We conclude that SHC interacts directly with the IR and that phosphorylation of Tyr-960 within the IR juxtamembrane domain is necessary for efficient interaction. This interaction is highly reminiscent of that of IRS-1 with the IR, and we show that the SHC IR-binding domain can substitute for that of IRS-1 in yeast and COS cells. We identify a homologous region within the IR-binding domains of SHC and IRS-1, which we term the SAIN (SHC and IRS-1 NPXY-binding) domain, which may explain the basis of these interactions. The SAIN domain appears to represent a novel motif which is able to interact with autophosphorylated receptors such as the IR. | lld:pubmed |
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| pubmed-article:7537849 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7537849 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7537849 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7537849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7537849 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7537849 | pubmed:month | May | lld:pubmed |
| pubmed-article:7537849 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:7537849 | pubmed:author | pubmed-author:HOMM | lld:pubmed |
| pubmed-article:7537849 | pubmed:author | pubmed-author:O'NeillT JTJ | lld:pubmed |
| pubmed-article:7537849 | pubmed:author | pubmed-author:GustafsonT... | lld:pubmed |
| pubmed-article:7537849 | pubmed:author | pubmed-author:CraparoAA | lld:pubmed |
| pubmed-article:7537849 | pubmed:author | pubmed-author:SchaubC DCD | lld:pubmed |
| pubmed-article:7537849 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7537849 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:7537849 | pubmed:owner | NLM | lld:pubmed |
