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Originally published In Press as doi:10.1074/jbc.M007197200 on January 29, 2001

J. Biol. Chem., Vol. 276, Issue 17, 14490-14497, April 27, 2001
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Phosphorylation of Protein Phosphatase Inhibitor-1 by Cdk5*

James A. BibbDagger §, Akinori Nishi, James P. O'Callaghan||, Jernej UleDagger , Martin LanDagger , Gretchen L. SnyderDagger , Atsuko HoriuchiDagger , Taro Saito**, Shin-ichi Hisanaga**, Andrew J. CzernikDagger , Angus C. NairnDagger , and Paul GreengardDagger

From the Dagger  Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, New York, New York 10021-6399, the  Department of Physiology, Kurume University School of Medicine, Kurume, Fukuoka, Japan 830-0011, the || Centers for Disease Control and Prevention, National Institute for Occupational Safety and Health, Morgantown, West Virginia 26505, and the ** Department of Biological Sciences, Graduate School of Science, Tokyo Metropolitan University, Tokyo, Japan 192-0397

Protein phosphatase inhibitor-1 is a prototypical mediator of cross-talk between protein kinases and protein phosphatases. Activation of cAMP-dependent protein kinase results in phosphorylation of inhibitor-1 at Thr-35, converting it into a potent inhibitor of protein phosphatase-1. Here we report that inhibitor-1 is phosphorylated in vitro at Ser-67 by the proline-directed kinases, Cdk1, Cdk5, and mitogen-activated protein kinase. By using phosphorylation state-specific antibodies and selective protein kinase inhibitors, Cdk5 was found to be the only kinase that phosphorylates inhibitor-1 at Ser-67 in intact striatal brain tissue. In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. The state of phosphorylation of inhibitor-1 at Ser-67 was dynamically regulated in striatal tissue by glutamate-dependent regulation of N-methyl-D-aspartic acid-type channels. Phosphorylation of Ser-67 did not convert inhibitor-1 into an inhibitor of protein phosphatase-1. However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation.

* This work was supported by a National Research Service award (to J. B.) and by the National Institute of Mental Health and the National Institute of Drug Abuse (to G. L. S., A. C. N., and P. G.).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.

This paper is dedicated to the memory of George Kuzmycs (1916-1996) whose contribution to the generation of polyclonal antibodies used in our laboratory has been and will continue to be an invaluable resource.

§ To whom correspondence should be addressed. E-mail: bibbj@rockvax.rockefeller.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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