pubmed-article:8413261 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8413261 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
pubmed-article:8413261 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:8413261 | lifeskim:mentions | umls-concept:C1334140 | lld:lifeskim |
pubmed-article:8413261 | lifeskim:mentions | umls-concept:C0123658 | lld:lifeskim |
pubmed-article:8413261 | lifeskim:mentions | umls-concept:C0282534 | lld:lifeskim |
pubmed-article:8413261 | lifeskim:mentions | umls-concept:C1160520 | lld:lifeskim |
pubmed-article:8413261 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
pubmed-article:8413261 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:8413261 | pubmed:dateCreated | 1993-11-18 | lld:pubmed |
pubmed-article:8413261 | pubmed:abstractText | Xenopus oocytes from unprimed frogs possess insulin-like growth factor I (IGF-I) receptors but lack insulin and IGF-I receptor substrate 1 (IRS-1), the endogenous substrate of this kinase, and fail to show downstream responses to hormonal stimulation. Microinjection of recombinant IRS-1 protein enhances insulin-stimulated phosphatidylinositol (PtdIns) 3-kinase activity and restores the germinal vesicle breakdown response. Activation of PtdIns 3-kinase results from formation of a complex between phosphorylated IRS-1 and the p85 subunit of PtdIns 3-kinase. Microinjection of a phosphonopeptide containing a pYMXM motif with high affinity for the src homology 2 (SH2) domain of PtdIns 3-kinase p85 inhibits IRS-1 association with and activation of the PtdIns 3-kinase. Formation of the IRS-1-PtdIns 3-kinase complex and insulin-stimulated PtdIns 3-kinase activation are also inhibited by microinjection of a glutathione S-transferase fusion protein containing the SH2 domain of p85. This effect occurs in a concentration-dependent fashion and results in a parallel loss of hormone-stimulated oocyte maturation. These inhibitory effects are specific and are not mimicked by glutathione S-transferase fusion proteins expressing the SH2 domains of ras-GAP or phospholipase C gamma. Moreover, injection of the SH2 domains of p85, ras-GAP, and phospholipase C gamma do not interfere with progesterone-induced oocyte maturation. These data demonstrate that phosphorylation of IRS-1 plays an essential role in IGF-I and insulin signaling in oocyte maturation and that this effect occurs through interactions of the phosphorylated YMXM/YXXM motifs of IRS-1 with SH2 domains of PtdIns 3-kinase or some related molecules. | lld:pubmed |
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pubmed-article:8413261 | pubmed:language | eng | lld:pubmed |
pubmed-article:8413261 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8413261 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8413261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8413261 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8413261 | pubmed:month | Nov | lld:pubmed |
pubmed-article:8413261 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:8413261 | pubmed:author | pubmed-author:KahnC RCR | lld:pubmed |
pubmed-article:8413261 | pubmed:author | pubmed-author:BackerJ MJM | lld:pubmed |
pubmed-article:8413261 | pubmed:author | pubmed-author:BirnbaumM JMJ | lld:pubmed |
pubmed-article:8413261 | pubmed:author | pubmed-author:WhiteM FMF | lld:pubmed |