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Originally published In Press as doi:10.1074/jbc.M209335200 on October 21, 2002

J. Biol. Chem., Vol. 277, Issue 51, 49605-49612, December 20, 2002
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A Novel Transmembrane Ser/Thr Kinase Complexes with Protein Phosphatase-1 and Inhibitor-2*

Hong Wang and David L. BrautiganDagger

From the Center for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia 22908-0577

Protein kinases and protein phosphatases exert coordinated control over many essential cellular processes. Here, we describe the cloning and characterization of a novel human transmembrane protein KPI-2 (Kinase/Phosphatase/Inhibitor-2) that was identified by yeast two-hybrid using protein phosphatase inhibitor-2 (Inh2) as bait. KPI-2 mRNA was predominantly expressed in skeletal muscle. KPI-2 is a 1503-residue protein with two predicted transmembrane helices at the N terminus, a kinase domain, followed by a C-terminal domain. The transmembrane helices were sufficient for targeting proteins to the membrane. KPI-2 kinase domain has about 60% identity with its closest relative, a tyrosine kinase. However, it only exhibited serine/threonine kinase activity in autophosphorylation reactions or with added substrates. KPI-2 kinase domain phosphorylated protein phosphatase-1 (PP1C) at Thr320, which attenuated PP1C activity. KPI-2 C-terminal domain directly associated with PP1C, and this required a VTF motif. Inh2 associated with KPI-2 C-terminal domain with and without PP1C. Thus, KPI-2 is a kinase with sites to associate with PP1C and Inh2 to form a regulatory complex that is localized to membranes.

* This work was supported by a United States Public Health Service Grant GM56362 from the National Institutes of General Medical Sciences.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY130988.

Dagger To whom correspondence should be addressed: Center for Cell Signaling, University of Virginia School of Medicine, P. O. Box 800577, Charlottesville, VA 22908-0577. Tel.: 434-924-5892; Fax: 434-243-2829; E-mail: db8g@virginia.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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