Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.273.50.33864
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dc.titleGrowth hormone stimulates the formation of a multiprotein signaling complex involving p130(Cas) and CrkII: Resultant activation of c-Jun N- terminal kinase/stress-activated protein kinase (JNK/SAPK)
dc.contributor.authorZhu, T.
dc.contributor.authorGoh, E.L.K.
dc.contributor.authorLeRoith, D.
dc.contributor.authorLobie, P.E.
dc.date.accessioned2014-11-28T02:51:02Z
dc.date.available2014-11-28T02:51:02Z
dc.date.issued1998-12-11
dc.identifier.citationZhu, T., Goh, E.L.K., LeRoith, D., Lobie, P.E. (1998-12-11). Growth hormone stimulates the formation of a multiprotein signaling complex involving p130(Cas) and CrkII: Resultant activation of c-Jun N- terminal kinase/stress-activated protein kinase (JNK/SAPK). Journal of Biological Chemistry 273 (50) : 33864-33875. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.273.50.33864
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/111909
dc.description.abstractWe have demonstrated previously that growth hormone (GH) activates focal adhesion kinase (FAK), and this activation results in the tyrosine phosphorylation of two FAK substrates, namely paxillin and tensin. We now show here in Chinese hamster ovary cells stably transfected with rat GH receptor cDNA that human (h)GH induces the formation of a large multiprotein signaling complex centered around another FAK-associated protein, p130(Cas) and the adaptor protein CrkII. hGH stimulates the tyrosine phosphorylation of both p130(Cas) and CrkII, their association, and the association of multiple other tyrosine-phosphorylated proteins to the complex. Both the c-Src and c- Fyn tyrosine kinases are tyrosine phosphorylated and activated by cellular hGH stimulation and form part of the multiprotein signaling complex as does tensin, paxillin, IRS-1, the p85 subunit of phosphatidylinositol 3-kinase, C3G, SHC, Grb-2, and Sos-1. c-Cbl and Nck are also tyrosine-phosphorylated by cellular stimulation with hGH and associate with the p130(Cas)-CrkII complex. c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) is activated in response to hGH in accordance with the formation of the abovementioned signaling complex, and hGH stimulated JNK/SAPK activity is increased in CrkII overexpressing NIH3T3 cells compared with vector transfected NIH3T3 cells. The formation of such a large multiprotein signaling complex by GH, with the resultant activation of multiple downstream effector molecules, may be central to many of the pleiotropic effects of GH.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.273.50.33864
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentINSTITUTE OF MOLECULAR & CELL BIOLOGY
dc.description.doi10.1074/jbc.273.50.33864
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume273
dc.description.issue50
dc.description.page33864-33875
dc.description.codenJBCHA
dc.identifier.isiut000077462500108
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