title: Phospholipase D structure and regulation.
abstract: The recent identification of cDNA clones for phospholipase D has opened the door to new types of investigations into its structure and regulation. PLD activity has been found to be 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 multiples steps in regulated secretion and membrane biogenesis.
authors.affiliation: Department of Pharmacological Sciences, SUNY at Stony Brook 11794-8651, USA. michael@pharm.som.sunysb.edu
authors.forename: M A
authors.initials: MA
authors.lastname: Frohman
authors.forename: A J
authors.initials: AJ
authors.lastname: Morris
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D018076:DNA, Complementary; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D008969:Molecular Sequence Data; D010739:Phospholipase D / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D018076:DNA, Complementary; D011994:Recombinant Proteins; D010727:Phosphoric Diester Hydrolases; D010739:Phospholipase D