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Regulation of phospholipase D Exton JHFEBS Lett 2002[Oct]; 531 (1): 58-61Structural studies of plant and bacterial members of the phospholipase D (PLD) superfamily are providing information about the role of the conserved HKD domains in the structure of the catalytic center and the catalytic mechanism of mammalian PLD isozymes (PLD1 and PLD2). Mutagenesis and sequence comparison studies have also defined the presence of pleckstrin homology and phox homology domains in the N-terminus and have demonstrated that a conserved sequence at the C-terminus is required for catalysis. The N- and C-terminal regions of PLD1 also contain interaction sites for protein kinase C, which can directly activate the enzyme through a non-phosphorylating mechanism. Small G proteins of the Rho and ADP-ribosylation factor families also directly regulate the enzyme, with RhoA binding to a sequence in the C-terminus. Certain tyrosine kinases and members of the Ras subfamily of small G proteins can activate the enzyme, but the mechanisms appear to be indirect. The mechanisms by which agonists activate PLD in vivo probably involve multiple pathways.|*Gene Expression Regulation, Enzymologic[MESH]|ADP-Ribosylation Factors/metabolism[MESH]|Animals[MESH]|Binding Sites[MESH]|Catalysis[MESH]|GTP-Binding Proteins/metabolism[MESH]|Humans[MESH]|Phospholipase D/*metabolism/*physiology[MESH]|Phosphorylation[MESH]|Protein Binding[MESH]|Protein Conformation[MESH]|Protein Isoforms[MESH]|Protein Kinase C/metabolism[MESH]|Protein Structure, Tertiary[MESH]|Protein-Tyrosine Kinases/metabolism[MESH]|Tyrosine/metabolism[MESH]|rhoA GTP-Binding Protein/metabolism[MESH] |
