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Originally published In Press as doi:10.1074/jbc.M207833200 on September 26, 2002

J. Biol. Chem., Vol. 277, Issue 50, 48796-48802, December 13, 2002
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Mapping the Protein Phosphatase-2B Anchoring Site on AKAP79
BINDING AND INHIBITION OF PHOSPHATASE ACTIVITY ARE MEDIATED BY RESIDUES 315-360*

Mark L. Dell'AcquaDagger §, Kimberly L. DodgeDagger , Steven J. TavalinDagger ||, and John D. ScottDagger **

From the Dagger  Howard Hughes Medical Institute, Vollum Institute, Oregon Health Sciences University, Portland, Oregon 97201 and the § Department of Pharmacology, School of Medicine, University of Colorado Health Sciences Center, Denver, Colorado 80262

Compartmentalization of protein kinases and phosphatases with substrates is a means to increase the efficacy of signal transduction events. The A-kinase anchoring protein, AKAP79, is a multivalent anchoring protein that maintains the cAMP-dependent protein kinase, protein kinase C, and protein phosphatase-2B (PP2B/calcineurin) at the postsynaptic membrane of excitatory synapses where it is recruited into complexes with N-methyl-D-aspartic acid or alpha -amino-3-hydroxy-5-methyl-isoxazole-4-propionic acid (AMPA)-subtype glutamate receptors. We have used cellular targeting of AKAP79 truncation and deletion mutants as an assay to map the PP2B-binding site on AKAP79. We demonstrate that residues 315-360 are necessary and sufficient for AKAP79-PP2B anchoring in cells. Multiple determinants contained within this region bind directly to the A subunit of PP2B and inhibit phosphatase activity. Peptides spanning the 315-360 region of AKAP79 can antagonize PP2B anchoring in vitro and targeting in transfected cells. Electrophysiological experiments further emphasize this point by demonstrating that a peptide encompassing residues 330-357 of AKAP79 attenuates PP2B-dependent down-regulation of GluR1 receptor currents when perfused into HEK293 cells. We propose that the structural features of this AKAP79-PP2B-binding domain may share similarities with other proteins that serve to coordinate PP2B localization and activity.

* This work was supported in part by Scientist Development Grant AHA-SDG 0130228N from the American Heart Association (to M. L. D.) and National Institutes of Health Grant GM48231 (to J. D. S.).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.

Both authors contributed equally to this work.

|| Present address: Dept. of Pharmacology, College of Medicine, University of Tennessee Health Science Center, Memphis, TN 38163.

** To whom correspondence should be addressed. E-mail: scott@ohsu.edu.

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