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Proc Natl Acad Sci U S A 1991 Jun 01;8811:4981-5. doi: 10.1073/pnas.88.11.4981.
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Mitogen-activated Swiss mouse 3T3 RSK kinases I and II are related to pp44mpk from sea star oocytes and participate in the regulation of pp90rsk activity.

Chung J , Pelech SL , Blenis J .

Using a recombinant rsk gene product as a substrate for in vitro kinase assays, we have identified two mitogen-activated Swiss 3T3 RSK protein kinase activities (referred to as RSK kinase I and RSK kinase II, based on their order of elution from phenyl-Sepharose). Polyclonal antisera prepared against maturation-regulated 44-kDa myelin basic protein (MBP) kinase (pp44mpk) purified from sea star oocytes demonstrated immunocrossreactivity with polypeptides of approximately 44 kDa in the RSK kinase I preparation and approximately 42 kDa in the RSK kinase II preparation, respectively. These polypeptides were also recognized by anti-phosphotyrosine antibodies, and either phosphatase 1B or 2A (tyrosine- and serine/threonine-specific phosphatases, respectively) separately inactivated RSK phosphotransferase activity supporting the notion that tyrosine and serine/threonine phosphorylation are required for activity. In vitro, both RSK kinases and MBP kinase phosphorylated recombinant RSK and generated nearly identical two-dimensional tryptic phosphopeptide maps. They also phosphorylated MBP and microtubule-associated protein 2 but not 40S ribosomal protein S6. Furthermore, these protein kinases phosphorylated and partially activated pp90rsk in immune complexes obtained from quiescent cells.

PubMed ID: 2052581
PMC ID: PMC51791
Article link: Proc Natl Acad Sci U S A
Grant support: [+]

Genes referenced: LOC100887844 LOC586799 rps6

References [+] :
Ahn, Evidence for an epidermal growth factor-stimulated protein kinase cascade in Swiss 3T3 cells. Activation of serine peptide kinase activity by myelin basic protein kinases in vitro. 1990, Pubmed