INTERACTION OF RAC WITH P67(PHOX) AND REGULATION OF PHAGOCYTIC NADPH OXIDASE ACTIVITY

被引:345
作者
DIEKMANN, D
ABO, A
JOHNSTON, C
SEGAL, AW
HALL, A
机构
[1] UCL, CANC RES CAMPAIGN,ONCOGENE & SIGNAL TRANSDUCT GRP, MRC,MOLEC & CELL BIOL LAB, LONDON WC1E 6BT, ENGLAND
[2] UCL, DEPT BIOCHEM, LONDON WC1E 6BT, ENGLAND
[3] UCL, DEPT MED, LONDON WC1E 6JJ, ENGLAND
基金
英国惠康基金;
关键词
D O I
10.1126/science.8036496
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Rho and Rac, two members of the Ras superfamily of guanosine triphosphate (GIP)-binding proteins, regulate a variety of signal transduction pathways in eukaryotic cells. Upon stimulation of phagocytic cells, Rac enhances the activity of the enzyme nicotinamide adenine dinucleotide phosphate (reduced) (NADPH) oxidase, resulting in the production of superoxide radicals. Activation of the NADPH oxidase requires the assembly of a multimolecular complex at the plasma membrane consisting of two integral membrane proteins, gp91(phox) and p2l(phox), and two cytosolic proteins, p67(phox) and p47(phox). Rac1 interacted directly with p67(phox) in GTP-dependent manner. Modified forms of Rac with mutations in the effector site did not stimulate oxidase activity or bind to p67(phox). Thus, p67(phox) appears to be the Rac effector protein in the NADPH oxidase complex.
引用
收藏
页码:531 / 533
页数:3
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