Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II - PubMed (original) (raw)

. 1988 Aug 25;334(6184):715-8.

doi: 10.1038/334715a0.

Affiliations

• PMID: 2842685
• DOI: 10.1038/334715a0

Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II

T W Sturgill et al. Nature. 1988.

Abstract

Ribosomal protein S6 is a component of the eukaryotic 40S ribosomal subunit that becomes phosphorylated on multiple serine residues in response to a variety of mitogens, including insulin, growth factors, and transforming proteins of many oncogenic viruses. Recently, an activated S6 kinase (S6 K II) has been purified to homogeneity from Xenopus eggs, and characterized immunologically and at the molecular level. Purified S6 K II can be deactivated in vitro by incubation with either protein phosphatase 1 or protein phosphatase 2A. Reactivation and phosphorylation of S6 K II occurs in vitro with an insulin-stimulated microtubule-associated protein-2 (MAP-2) protein kinase which is itself a phosphoprotein that can be deactivated by protein phosphatase 2A. These studies suggest that a step in insulin signalling involves sequential activation by phosphorylation of at least two serine/threonine protein kinases.

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