Phorbol myristate acetate-dependent association of protein kinase C alpha with phospholipase D1 in intact cells.
A phospholipase D1 (PLD1) was purified from rat brain by the use of antibody-coupled protein A Sepharose. We found that protein kinase C alp (PKCalpha) stimulated PLD1 activity in the presence of phorbol myristate acetate (PMA). PMA-dependent association of PKCalpha with PLD1 was verified in NIH-3T3 fibroblast cells, and COS7 cells transiently expressing PLD1 as well as in vitro suggesting that the activation of PLD1 resulted from direct association of PKCalpha with PLD1.
Lee
T G
TG
Department of Life Science, Pohang University of Science and Technology, South Korea.
Park
J B
JB
Lee
S D
SD
Hong
S
S
Kim
J H
JH
Kim
Y
Y
Yi
K S
KS
Bae
S
S
Hannun
Y A
YA
Obeid
L M
LM
Suh
P G
PG
Ryu
S H
SH
D016475:3T3 Cells; D000818:Animals; D001921:Brain / Q000201:enzymology; D019556:COS Cells; D004789:Enzyme Activation; D051379:Mice; D010739:Phospholipase D / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D011493:Protein Kinase C; D010739:Phospholipase D; C106801:phospholipase D1; D013755:Tetradecanoylphorbol Acetate