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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Cardiac phospholipase D-2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner

Cited 100 times inthomson ciCited 97 times inthomson ci
Title
Cardiac phospholipase D-2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner
Author
Park, Jong BaeKim, Jung HwanKim, YongHa, Sang HoonKim, Jae HoYoo, JSDu, GWFrohman, MASuh, Pann-GhillRyu, SH
Issue Date
2000-07
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.275, no.28, pp.21295 - 21301
Abstract
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 (Ic(50) = 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
URI
https://scholarworks.unist.ac.kr/handle/201301/16527
URL
http://www.jbc.org/content/275/28/21295.long
DOI
10.1074/jbc.M002463200
ISSN
0021-9258
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