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Originally published In Press as doi:10.1074/jbc.M002463200 on May 2, 2000

J. Biol. Chem., Vol. 275, Issue 28, 21295-21301, July 14, 2000
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Cardiac Phospholipase D2 Localizes to Sarcolemmal Membranes and Is Inhibited by alpha -Actinin in an ADP-ribosylation Factor-reversible Manner*

Jong Bae ParkDagger , Jung Hwan KimDagger , Yong KimDagger , Sang Hoon HaDagger , Jae Ho KimDagger , Jong-Shin Yoo§, Guangwei Du, Michael A. Frohman, Pann-Ghill SuhDagger , and Sung Ho RyuDagger ||

From the Dagger  Department of Life Science and Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea, the § Mass Spectrometry Analysis Group, Korea Basic Science Institute, Taejon 305-333, Korea, and the  Department of Pharmacology and the Institute for Cell and Developmental Biology, State University of New York, Stony Brook, New York 11794-8651

Myocardial phospholipase D (PLD) has been implicated in the regulation of Ca2+ mobilization and contractile performance in the heart. However, the molecular identity of this myocardial PLD and the mechanisms that regulate it are not well understood. Using subcellular fractionation and Western blot analysis, we found that PLD2 is the major myocardial PLD and that it localizes primarily to sarcolemmal membranes. A 100-kDa PLD2-interacting cardiac protein was detected using a protein overlay assay employing purified PLD2 and then identified as alpha -actinin using peptide-mass fingerprinting with matrix-assisted laser desorption/ionization mass spectroscopy. The direct association between PLD2 and alpha -actinin was confirmed using an in vitro binding assay and localized to PLD2's N-terminal 185 amino acids. Purified alpha -actinin potently inhibits PLD2 activity (IC50 = 80 nM) in an interaction-dependent and ADP-ribosylation factor-reversible manner. Finally, alpha -actinin co-localizes with actin and with PLD2 in the detergent-insoluble fraction from sarcolemmal membranes. These results suggest that PLD2 is reciprocally regulated in sarcolemmal membranes by alpha -actinin and ARF1 and accordingly that a major role for PLD2 in cardiac function may involve reorganization of the actin cytoskeleton.

* This work was supported by grants from the National Research Laboratory and Brain Research of Ministry of Science and Technology and the Center for Cell Signalling Research in the Republic of Korea (to S. H. R.) and by National Institutes of Health Grant GM54813 (to M. A. F.).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. Tel.: 82-562-279-5971; Fax: 82-562-279-2199; E-mail: sungho@postech.ac.kr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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