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Originally published In Press as doi:10.1074/jbc.M206960200 on September 21, 2002

J. Biol. Chem., Vol. 277, Issue 48, 46535-46543, November 29, 2002
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Neurabins Recruit Protein Phosphatase-1 and Inhibitor-2 to the Actin Cytoskeleton*

Ryan T. Terry-Lorenzo, Elizabeth ElliotDagger , Douglas C. Weiser, Todd D. PrickettDagger , David L. BrautiganDagger , and Shirish Shenolikar§

From the Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710 and Dagger  Center for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia 22908

Inhibitor-2 (I-2) bound protein phosphatase-1 (PP1) and several PP1-binding proteins from rat brain extracts, including the actin-binding proteins, neurabin I and neurabin II. Neurabins from rat brain lysates were sedimented by I-2 and its structural homologue, I-4. The central domain of both neurabins bound PP1 and I-2, and mutation of a conserved PP1-binding motif abolished neurabin binding to both proteins. Microcystin-LR, a PP1 inhibitor, also attenuated I-2 binding to neurabins. Immunoprecipitation of neurabin I established its association with PP1 and I-2 in HEK293T cells and suggested that PP1 mediated I-2 binding to neurabins. The C terminus of I-2, although not required for PP1 binding, facilitated PP1 recruitment by neurabins, which also targeted I-2 to polymerized F-actin. Mutations that attenuated PP1 binding to I-2 and neurabin I suggested distinct and overlapping sites for these two proteins on the PP1 catalytic subunit. Immunocytochemistry in epithelial cells and cultured hippocampal neurons showed that endogenous neurabin II and I-2 colocalized at actin-rich structures, consistent with the ability of neurabins to target the PP1·I-2 complex to actin cytoskeleton and regulate cell morphology.

* This work was supported by National Institutes of Health Grants NS41063 (to S. S.) and GM56362 (to D. L. B.) and National Science Foundation Graduate Research Fellowship (to R. T. T.-L.).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.

§ To whom correspondence should be addressed: Dept. of Pharmacology and Cancer Biology, Duke University Medical Center, LSRC C315, Research Dr., Durham, NC 27710. Tel.: 919-681-6178; Fax: 919-681-9567; E-mail: sheno001@mc.duke.edu.

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