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PLD1 stimulates actin polymerization in lipase activity‐independent manner.
Author(s) -
You Won,
Lee Jun Sung,
Ryu Sung Ho
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a482-c
Subject(s) - actin , phosphatidic acid , microbiology and biotechnology , mdia1 , polymerization , actin binding protein , chemistry , actin remodeling of neurons , phospholipase d , actin remodeling , lamellipodium , actin cytoskeleton , biophysics , biology , biochemistry , cytoskeleton , phospholipid , polymer , cell , signal transduction , organic chemistry , membrane
The regulation of actin dynamics is a pivotal process in cells. phospholipase D (PLD)1 has been suggested to be involved in the actin polimerization, but the mechamism of regulation is still unclear. In this study, we report that PLD1 binds directly to neural Wiskott–Aldrich syndrome protein (N‐WASP), which is an actin nucleation stimulator, and induces actin polymerization in lipase activity‐independent manner. Strikingly, we also found that phosphatidic acid(PA) functions in the maintenance of actin filament, rather than initiation of actin polimerization. Taken together, we demonstrate the role of PLD1 in actin polymerization in molecular level, and suggest the involvement of PA in actin dynamics regulation.