Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta.

作者: Lars-Oliver Essen , Olga Perisic , Robert Cheung , Matilda Katan , Roger L. Williams

DOI: 10.1038/380595A0

关键词:

摘要: Mammalian phosphoinositide-specific phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The 2.4-A structure of delta 1 reveals a multidomain protein incorporating modules shared by many signalling proteins. suggests mechanism for membrane attachment Ca2+-dependent hydrolysis second-messenger precursors. regulation reversible association PI-PLC may serve model understanding other involved in phospholipid signalling.

参考文章(42)
D. W. Heinz, M. Ryan, T. L. Bullock, O. H. Griffith, Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol. The EMBO Journal. ,vol. 14, pp. 3855- 3863 ,(1995) , 10.1002/J.1460-2075.1995.TB00057.X
S.G. Rhee, K.D. Choi, Regulation of inositol phospholipid-specific phospholipase C isozymes. Journal of Biological Chemistry. ,vol. 267, pp. 12393- 12396 ,(1992) , 10.1016/S0021-9258(18)42284-3
Maria E Cifuentes, L Honkanen, MJ Rebecchi, None, Proteolytic fragments of phosphoinositide-specific phospholipase C-delta 1. Catalytic and membrane binding properties. Journal of Biological Chemistry. ,vol. 268, pp. 11586- 11593 ,(1993) , 10.1016/S0021-9258(19)50241-1
H Yagisawa, H Kamata, Y Watanabe, M Hirata, S Ozaki, H Hirata, N Yabuta, K Sakuma, H Tanaka, T Kanematsu, Expression and characterization of an inositol 1,4,5-trisphosphate binding domain of phosphatidylinositol-specific phospholipase C-delta 1. Journal of Biological Chemistry. ,vol. 269, pp. 20179- 20188 ,(1994) , 10.1016/S0021-9258(17)32143-9
Stephen J. Taylor, Ho Zoon Chae, Sue Goo Rhee, John H. Exton, Activation of the beta 1 isozyme of phospholipase C by alpha subunits of the Gq class of G proteins. Nature. ,vol. 350, pp. 516- 518 ,(1991) , 10.1038/350516A0
O. Hayes Griffith, Johannes J. Volwerk, Andreas Kuppe, Phosphatidylinositol-specific phospholipases C from Bacillus cereus and Bacillus thuringiensis Methods in Enzymology. ,vol. 197, pp. 493- 502 ,(1991) , 10.1016/0076-6879(91)97175-X
A.L. Drayer, P.J. van Haastert, Molecular Cloning and Expression of a Phosphoinositide-specific Phospholipase C of Dictyostelium discoideum Journal of Biological Chemistry. ,vol. 267, pp. 18387- 18392 ,(1992) , 10.1016/S0021-9258(19)36974-1
J Moult, M N James, O Herzberg, A model for the Ca2+-induced conformational transition of troponin C. A trigger for muscle contraction. Journal of Biological Chemistry. ,vol. 261, pp. 2638- 2644 ,(1986) , 10.1016/S0021-9258(17)35835-0
L A Serunian, M T Haber, T Fukui, J W Kim, S G Rhee, J M Lowenstein, L C Cantley, Polyphosphoinositides produced by phosphatidylinositol 3-kinase are poor substrates for phospholipases C from rat liver and bovine brain. Journal of Biological Chemistry. ,vol. 264, pp. 17809- 17815 ,(1989) , 10.1016/S0021-9258(19)84645-8
M.A. Swairjo, N.O. Concha, M.A. Kaetzel, J.R. Dedman, B.A. Seaton, Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nature Structural & Molecular Biology. ,vol. 2, pp. 968- 974 ,(1995) , 10.1038/NSB1195-968