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α 1 ‐Adrenergic receptor‐induced cytoskeletal organization and cell motility in CCL39 fibroblasts requires phospholipase D1
Author(s) -
Wallert M.,
McCoy A.,
Voog J.,
Rastedt D.,
TavesPatterson J.,
KorpiSteiner N.,
Canine J.,
Ngyuen T.,
Nguyen C.,
Provost J.
Publication year - 2011
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.23227
Subject(s) - stress fiber , phospholipase d , pld2 , microbiology and biotechnology , rhoa , mapk/erk pathway , cytoskeleton , motility , rac1 , chemistry , phosphatidic acid , phosphorylation , signal transduction , focal adhesion , biology , cell , biochemistry , phospholipid , membrane
The role of phospholipase D (PLD) in cytoskeletal reorganization, ERK activation, and migration is well established. Both isoforms of PLD (PLD1 and PLD2) can independently activate stress fiber formation and increase ERK phosphorylation. However, the isoform's specificity, upstream activators, and downstream targets of PLD that coordinate this process are less well understood. This study explores the role of α 1 ‐adrenergic receptor stimulation and its effect on PLD activity. We demonstrate that PLD1 activators, RhoA, and PKCα are critical for stress fiber formation and ERK activation, and enhance the production of phosphatidic acid (PA) upon phenylephrine addition. Ectopic expression of dominant negative PLD1 and not PLD2 blocks ERK activation, inhibits stress fiber formation, and reduces cell motility in CCL39 fibroblasts. Furthermore, we demonstrate the mechanism for PLD1 activation of ERK involves Ras. This work indicates that PLD1 plays a novel role mediating growth factor and cell motility events in α 1 ‐adrenergic receptor‐activated cells. J. Cell. Biochem. 112: 3025–3034, 2011. © 2011 Wiley‐Liss, Inc.