Evidence for Two Catalytically Active Kinase Domains in pp90rsk
Open Access
- 1 March 1996
- journal article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 16 (3) , 1212-1219
- https://doi.org/10.1128/mcb.16.3.1212
Abstract
Mitogen-activated protein kinase and one of its targets, pp90rsk (ribosomal S6 kinase [RSK]), represent two serine/threonine kinases in the Ras-activated signalling cascade that are capable of directly regulating gene expression. pp90rsk has been shown to have two highly conserved and distinct catalytic domains. However, whether both domains are active and which domain is responsible for its various identified phosphotransferase activities have not been determined. Here we demonstrate that the N-terminal domain is responsible for its phosphotransferase activity towards a variety of substrates which contain an RXXS motif at the site of in vitro phosphorylation, including serum response factor, c-Fos, Nur77, and the 40S ribosomal protein S6. We also provide evidence that the C-terminal domain is catalytically active and can be further activated by mitogen-activated protein kinase phosphorylation.Keywords
This publication has 36 references indexed in Scilit:
- [19] Rapid and efficient site-specific mutagenesis without phenotypic selectionPublished by Elsevier ,2004
- Three protein kinase structures define a common motifStructure, 1994
- S6 Phosphorylation and the p70s6k/p85s6kCritical Reviews in Biochemistry and Molecular Biology, 1994
- The Primary Structure of MEK, a Protein Kinase that Phosphorylates the ERK Gene ProductScience, 1992
- Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinasesCell, 1992
- Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activityCell, 1991
- Identification of cell cycle-regulated phosphorylation sites on nuclear lamin CCell, 1990
- Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase IINature, 1988
- A Xenopus ribosomal protein S6 kinase has two apparent kinase domains that are each similar to distinct protein kinases.Proceedings of the National Academy of Sciences, 1988
- Construction and Characterization of a Retroviral Vector Demonstrating Efficient Expression of Cloned cDNA SequencesDNA, 1988