Mammalian phospholipase D structure and regulation.
The recent identification of cDNA clones for phospholipase D1 and 2 has opened the door to new studies on its structure and regulation. PLD activity is encoded by at least two different genes that contain catalytic domains that relate their mechanism of action to phosphodiesterases. In vivo roles for PLD suggest that it may be important for multiple specialized steps in receptor dependent and constitutive processes of secretion, endocytosis, and membrane biogenesis.
Frohman
M A
MA
Department of Pharmacological Sciences, Institute for Cell and Developmental Biology, SUNY at Stony Brook, Stony Brook, NY 1794-8651, USA. michael@pharm.som.sunysb.edu
Sung
T C
TC
Morris
A J
AJ
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D017124:Conserved Sequence; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D015971:Gene Expression Regulation, Enzymologic; D008322:Mammals / Q000235:genetics / Q000378:metabolism*; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000494:pharmacology; D010716:Phosphatidylinositols / Q000378:metabolism; D010739:Phospholipase D / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011493:Protein Kinase C / Q000494:pharmacology
D004791:Enzyme Inhibitors; D019269:Phosphatidylinositol 4,5-Diphosphate; D010716:Phosphatidylinositols; D011493:Protein Kinase C; D010739:Phospholipase D