DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chung, Jongkyeong | ko |
dc.date.accessioned | 2013-02-25T04:43:45Z | - |
dc.date.available | 2013-02-25T04:43:45Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1991-09 | - |
dc.identifier.citation | MOLECULAR AND CELLULAR BIOLOGY, v.11, no.4, pp.1868 - 1874 | - |
dc.identifier.issn | 0270-7306 | - |
dc.identifier.uri | http://hdl.handle.net/10203/59945 | - |
dc.description.abstract | Protein kinase assays that use recombinant pp90rsk as a substrate were developed in an attempt to identify growth-regulated enzymes responsible for the phosphorylation and activation of pp90rsk S6 phosphotransferase activity. With this assay we have identified a pp60v-src-, growth factor-, phorbol ester-, and vanadate-regulated serine/threonine protein kinase activity that is not related to two other cofactor-independent, growth-regulated protein kinases, pp70-S6 protein kinase and pp90rsk. The pp90rsk-protein kinase activity (referred to as rsk-kinase) is also not related to cofactor-dependent signal transducing protein kinases such as the cyclic AMP-dependent protein kinases, members of the protein kinase C family, or other Ca2+ -dependent protein kinases. In vitro, partially purified rsk-kinase phosphorylates several of the sites (serine and threonine) that are phosphorylated in growth-stimulated cultured cells. A detailed examination of the mitogen-regulated activation kinetics of rsk-kinase and pp90rsk activities demonstrated that they are coordinately regulated. In addition, protein kinase C is not absolutely required for epidermal and fibroblast growth factor-stimulated activation of rsk-kinase, whereas, like pp90rsk, platelet-derived growth factor- and vanadate-stimulated rsk-kinase activity exhibits a greater dependence on protein kinase C-mediated signal transduction. The characterization and future purification of the rsk-kinase(s) will improve our understanding of the early signaling events regulating cell growth. | - |
dc.language | English | - |
dc.publisher | Amer Soc Microbiology | - |
dc.subject | S6 KINASE | - |
dc.subject | INSULIN | - |
dc.subject | EXPRESSION | - |
dc.subject | ACTIVATION | - |
dc.subject | INVIVO | - |
dc.title | Coordinated regulation of pp90rsk and a distinct protein-serine/threonine kinase activity that phosphorylates recombinant pp90rsk in vitro. | - |
dc.type | Article | - |
dc.identifier.wosid | A1991FC85200012 | - |
dc.identifier.scopusid | 2-s2.0-0025924682 | - |
dc.type.rims | ART | - |
dc.citation.volume | 11 | - |
dc.citation.issue | 4 | - |
dc.citation.beginningpage | 1868 | - |
dc.citation.endingpage | 1874 | - |
dc.citation.publicationname | MOLECULAR AND CELLULAR BIOLOGY | - |
dc.contributor.localauthor | Chung, Jongkyeong | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | S6 KINASE | - |
dc.subject.keywordPlus | INSULIN | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | INVIVO | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.