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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.
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页数:11
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