Show simple item record

dc.contributor.authorNew, L.zh_CN
dc.contributor.authorZhao, M.zh_CN
dc.contributor.authorLi, Y. Q.zh_CN
dc.contributor.authorBassett, W. W.zh_CN
dc.contributor.authorFeng, Y.zh_CN
dc.contributor.authorLudwig, S.zh_CN
dc.contributor.authorPadova, F. D.zh_CN
dc.contributor.authorGram, H.zh_CN
dc.contributor.authorHan, J. H.zh_CN
dc.contributor.author韩家淮zh_CN
dc.date.accessioned2013-12-12T02:24:43Z
dc.date.available2013-12-12T02:24:43Z
dc.date.issued1999zh_CN
dc.identifier.citationJournal of Biological Chemistry,274(2):1026-1032zh_CN
dc.identifier.issn0021-9258zh_CN
dc.identifier.otherISI:000077968500062zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/65820
dc.description.abstractA novel protein kinase whose activity can be stimulated by mitogen in vivo was cloned and characterized. The cDNA of this gene encodes an 802-amino acid protein (termed RLPK) with the highest homology (37% identity) to the two protein kinase families, p90(RSK) and p70(RSK). Like p90(RSR), but not p70(RSK), RLPK also contains two complete nonidentical protein kinase domains. RLPK mRNA is widely expressed in all human tissues examined and is enriched in the brain, heart, and placenta. In HeLa cells, transiently expressed epitope-tagged RLPK can be strongly induced by epidermal growth factor, serum, and phorbol 12-myristate 13-acetate, but only moderately up-regulated by tumor necrosis factor-ct and other stress-related stimuli. The activity of RLPK stimulated by epidermal growth factor was not inhibited by several known protein kinase C inhibitors nor by rapamycin, a known specific inhibitor for p70(RSK), but could be inhibited by herbimycin A, a tyrosine kinase inhibitor, and partially inhibited by PD98059 or SB203580, inhibitors for the mitogen-activated protein kinase pathways. Recombinant RLPK possesses high phosphorylation activity toward histone 2B and the S6 peptide, RRRLSSLRA. Although purified recombinant RLPK can be phosphorylated by ERK2 and p38 alpha in vitro, its activity is not affected by this phosphorylation. Moreover, the treatment of RLPK with acid phosphatase did not reduce its in vitro kinase activity. These data suggest that RLPK is structurally similar to previously isolated RSKs, but its regulatory mechanism may be distinct from either p70(RSK) or p90(RSK)S.zh_CN
dc.language.isoen_USzh_CN
dc.subjectP70 S6 KINASEzh_CN
dc.subjectPHORBOL ESTERzh_CN
dc.subject2 ISOFORMSzh_CN
dc.subjectRAT-LIVERzh_CN
dc.subjectACTIVATIONzh_CN
dc.subjectPHOSPHORYLATIONzh_CN
dc.subjectPP90(RSK)zh_CN
dc.subjectRAPAMYCINzh_CN
dc.subjectPP90RSKzh_CN
dc.subjectDOMAINSzh_CN
dc.titleCloning and characterization of RLPK, a novel RSK-related protein kinasezh_CN
dc.typeArticlezh_CN


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record