PMID: 12761178May 23, 2003Paper

Regulation of type 1 protein phosphatase/inhibitor-2 complex by glycogen synthase kinase-3beta in intact cells

Journal of Biochemistry
Gyosuke SakashitaKunimi Kikuchi

Abstract

Inhibitor 2 (I-2) is a ubiquitous regulator of type 1 protein phosphatase (PP1). Previous in vitro studies suggested that its inhibitory activity towards PP1 is regulated by phosphorylation at Thr72 by glycogen synthase kinase-3beta (GSK-3beta), and at Ser86, Ser120, and Ser121 by casein kinase 2 (CK2). Here we report that GSK-3beta expressed in COS-7 cells phosphorylates wild-type I-2 but not an I-2 mutant carrying a T to A substitution at residue 72, showing that GSK-3beta phosphorylates I-2 at T72 in vivo as well. Co-immunoprecipitation study demonstrated that HA-GSK-3beta and I-2-FLAG co-exist in a same complex in the intact cells, but they do not bind directly. It is noteworthy that co-expression of Myc-PP1C significantly increased co-precipitation of HA-GSK-3beta with I-2-FLAG, showing a complex formation of HA-GSK-3beta/Myc-PP1C / I-2-FLAG in vivo. Further studies using a GSK-3beta kinase-dead mutant and LiCl, an inhibitor of GSK-3beta, showed that the enzyme activity of GSK-3beta is required for co-precipitation. IP-Western study using several I-2 mutants substituted at phosphorylation sites (T72, S86, S120, and S121) suggested that phosphorylation of I-2 by CK2 is also involved in enhancement of association between GSK...Continue Reading

Citations

Oct 29, 2008·Biochemistry·Barbara DancheckWolfgang Peti
Mar 11, 2009·Frontiers in Bioscience (Landmark Edition)·Persoulla Nicolaou, Evangelia G Kranias
Dec 3, 2014·Journal of Molecular and Cellular Cardiology·Kobra HaghighiEvangelia G Kranias
Feb 26, 2015·Journal of Neuroscience Research·John Fredy Castro-AlvarezGloria Patricia Cardona-Gómez

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