Phospholipase D: a lipid centric review

被引:385
作者
Jenkins, GM
Frohman, MA
机构
[1] SUNY Stony Brook, Dept Pharmacol, Med Ctr, Stony Brook, NY 11794 USA
[2] SUNY Stony Brook, Ctr Dev Genet, Med Ctr, Stony Brook, NY 11794 USA
关键词
phospholipase D; phosphatidic acid; diacylglercol; phosphatidylcholine; signal transduction;
D O I
10.1007/s00018-005-5195-z
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Phospholipase D (PLD) hydrolyzes the phosphodiester bond of the glycerolipid phosphatidylcholine, resulting in the production of phosphatidic acid and free choline. Phosphatidic acid is widely considered to be the intracellular lipid mediator of many of the biological functions attributed to PLD. However, phosphatidic acid is a tightly regulated lipid in cells and can be converted to other potentially bioactive lipids, including diacylglycerol and lysophosphatidic acid. PLD activities have been described in multiple organisms, including plants, mammals, bacteria and yeast. In mammalian systems, PLD activity regulates the actin cytoskeleton, vesicle trafficking for secretion and endocytosis, and receptor signaling. PLD is in turn regulated by phosphatidylinositol-4,5-bisphosphate, protein kinase C and ADP Ribosylation Factor and Rho family GTPases. This review focuses on the lipid precursors and products of mammalian PLD metabolism, especially phosphatidic acid and the roles this lipid performs in the mediation of the functions of PLD.
引用
收藏
页码:2305 / 2316
页数:12
相关论文
共 164 条
[51]   Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid - Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells [J].
Ghosh, S ;
Strum, JC ;
Sciorra, VA ;
Daniel, L ;
Bell, RM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (14) :8472-8480
[52]   Catalytic mechanism of the phospholipase D superfamily proceeds via a covalent phosphohistidine intermediate [J].
Gottlin, EB ;
Rudolph, AE ;
Zhao, Y ;
Matthews, HR ;
Dixon, JE .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (16) :9202-9207
[53]   CAPS acts at a prefusion step in dense-core vesicle exocytosis as a PIP2 binding protein [J].
Grishanin, RN ;
Kowalchyk, JA ;
Klenchin, VA ;
Kyougsook, A ;
Earles, CA ;
Chapman, ER ;
Gerona, RRL ;
Martin, TFJ .
NEURON, 2004, 43 (04) :551-562
[54]  
GUSTAVSSON L, 1994, J BIOL CHEM, V269, P849
[55]  
HAMMOND SM, 1995, J BIOL CHEM, V270, P29640
[56]   Characterization of two alternately spliced forms of phospholipase D1 - Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and RHO family monomeric GTP-binding proteins and protein kinase C-alpha [J].
Hammond, SM ;
Jenco, JM ;
Nakashima, S ;
Cadwallader, K ;
Gu, QM ;
Cook, S ;
Nozawa, Y ;
Prestwich, GD ;
Frohman, MA ;
Morris, AJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (06) :3860-3868
[57]  
HANAHAN DJ, 1947, J BIOL CHEM, V168, P233
[58]  
HANAHAN DJ, 1948, J BIOL CHEM, V172, P191
[59]   Phospholipase A2-mediated fusion of neutrophil-derived membranes is augmented by phosphatidic acid [J].
Harsh, DM ;
Blackwood, RA .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2001, 282 (02) :480-486
[60]  
HASLAM RJ, 1993, ADV EXP MED BIOL, V344, P149