pubmed-article:12374739 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12374739 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:12374739 | lifeskim:mentions | umls-concept:C0013710 | lld:lifeskim |
pubmed-article:12374739 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
pubmed-article:12374739 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
pubmed-article:12374739 | lifeskim:mentions | umls-concept:C0007586 | lld:lifeskim |
pubmed-article:12374739 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
pubmed-article:12374739 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
pubmed-article:12374739 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:12374739 | pubmed:issue | 20 | lld:pubmed |
pubmed-article:12374739 | pubmed:dateCreated | 2002-10-10 | lld:pubmed |
pubmed-article:12374739 | pubmed:abstractText | Microinjection in mouse eggs of tr-kit, a truncated form of the c-kit tyrosine kinase present in mouse spermatozoa, causes resumption of meiosis through activation of phospholipase Cgamma1 (PLCgamma1) and Ca(2+) mobilization from intracellular stores. We show that the Src-like kinase Fyn phosphorylates Tyr161 in tr-kit and that this residue is essential for tr-kit function. Fyn is localized in the cortex region underneath the plasma membrane in mouse oocytes. Using several approaches, we demonstrate that Fyn associates with tr-kit and that the interaction requires Tyr161. The interaction between tr-kit and Fyn triggers activation of the kinase as monitored by both autophosphorylation and phosphorylation of PLCgamma1. Co-injection of tr-kit with the SH2 domain of Fyn, or pre-treatment with a Fyn inhibitor, impairs oocyte activation, suggesting that activation of Fyn by tr-kit also occurs in vivo. Finally, microinjection of constitutively active Fyn triggers oocyte activation downstream of tr-kit but still requires PLC activity. We suggest that the mechanism by which tr-kit triggers resumption of meiosis of mouse eggs requires a functional interaction with Fyn and phosphorylation of PLCgamma1. | lld:pubmed |
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pubmed-article:12374739 | pubmed:language | eng | lld:pubmed |
pubmed-article:12374739 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12374739 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12374739 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12374739 | pubmed:month | Oct | lld:pubmed |
pubmed-article:12374739 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:12374739 | pubmed:author | pubmed-author:RossiPellegri... | lld:pubmed |
pubmed-article:12374739 | pubmed:author | pubmed-author:GeremiaRaffae... | lld:pubmed |
pubmed-article:12374739 | pubmed:author | pubmed-author:SetteClaudioC | lld:pubmed |
pubmed-article:12374739 | pubmed:author | pubmed-author:BarchiMarcoM | lld:pubmed |
pubmed-article:12374739 | pubmed:author | pubmed-author:BevilacquaArt... | lld:pubmed |
pubmed-article:12374739 | pubmed:author | pubmed-author:ParonettoMari... | lld:pubmed |
pubmed-article:12374739 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12374739 | pubmed:day | 15 | lld:pubmed |
pubmed-article:12374739 | pubmed:volume | 21 | lld:pubmed |
pubmed-article:12374739 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12374739 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12374739 | pubmed:pagination | 5386-95 | lld:pubmed |
pubmed-article:12374739 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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