The NADPH oxidase 2 subunit p47phox binds to the WAVE regulatory complex and p22phox in a mutually exclusive manner

被引:0
作者
Kuihon, Simon V. N. P. [1 ]
Sevart, Brodrick J. [1 ,3 ]
Abbey, Colette A. [2 ]
Bayless, Kayla J. [2 ]
Chen, Baoyu [1 ]
机构
[1] Iowa State Univ, Roy J Carver Dept Biochem Biophys & Mol Biol, Ames, IA 50011 USA
[2] Texas A&M Hlth Sci Ctr, Dept Med Physiol, Bryan, TX USA
[3] Colorado Sch Mines, NREL Adv Energy Syst Grad Program, 1500 Illinois St, Golden, CO 80401 USA
基金
美国国家卫生研究院;
关键词
REDOX REGULATION; ACTIN CYTOSKELETON; DOMAIN; ACTIVATION; PHOSPHORYLATION; MECHANISMS; PHYSIOLOGY; MIGRATION; PROTEIN; GTPASES;
D O I
10.1016/j.jbc.2024.107130
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
The actin cytoskeleton and reactive oxygen species (ROS) both play crucial roles in various cellular processes. Previous research indicated a direct interaction between two key components of these systems: the WAVE1 subunit of the WAVE regulatory complex (WRC), which promotes actin polymerization and the p47phoxsubunit of the NADPH oxidase 2 complex (NOX2), Src homology 3 domains to bind to multiple regions within the WAVE1 and Abi2 subunits of the WRC, without altering WRC's activity in promoting Arp2/3-mediated actin polymerization. Notably, contrary to previous findings, p47phox uses the same binding pocket to interact with both the WRC and the p22phox subunit of NOX2, albeit in a mutually exclusive manner. This participate in two distinct processes: assembling into NOX2 to promote ROS production and engaging with WRC to regulate the actin cytoskeleton.
引用
收藏
页数:11
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