Assembly of the neutrophil respiratory burst oxidase:: A direct interaction between p67PHOX and cytochrome b558 II

被引:70
作者
Dang, PMC
Cross, AR
Quinn, MT
Babior, BM [1 ]
机构
[1] Scripps Res Inst, Res Inst, Dept Mol & Expt Med, La Jolla, CA 92037 USA
[2] Montana State Univ, Dept Vet Mol Biol, Bozeman, MT 59717 USA
关键词
D O I
10.1073/pnas.072345299
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
Activation of the phagocyte NADPH oxidase complex requires assembly of the cytosolic factors p47(PHOX), p67(PHOX) p40(PHOX) and Rac with the membrane-bound cytochrome b(558). We recently established a direct interaction between p67(PHOX) and cytochrome b(558). In the present study, we show that removal of the C-terminal domain of p67(PHOX) increased its binding to cytochrome b558. Whereas phosphorylated p40(PHOX) alone did not bind to cytochrome b558, phosphorylated p47(PHOX) did, and, moreover, it allowed the binding of p40(PHOX) to the cytochrome. Furthermore, both increased the binding of p67(PHOX) to the cytochrome. Phosphorylated p47(PHOX) thus appears to increase the binding of p67(PHOX) to cytochrome b(558) by serving as an adapter, bringing p67(PHOX) into proximity with cytochrome b558, whereas phosphorylated p40(PHOX) may increase the binding by inducing a conformational change that allows p67(PHOX) to interact fully with cytochrome b(558).
引用
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页码:4262 / 4265
页数:4
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