Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 76, Issue 17, Pages 3349-3361Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-019-03128-y
Keywords
Actin cytoskeleton; Adhesion; Migration; Cortactin; Vesicle trafficking; Endosome; Cofilin; CK666
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Funding
- Mexican National Council for Science and Technology (Conacyt) [284292]
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The actin-related protein complex 2/3 (Arp2/3) generates branched actin networks important for many cellular processes such as motility, vesicular trafficking, cytokinesis, and intercellular junction formation and stabilization. Activation of Arp2/3 requires interaction with actin nucleation-promoting factors (NPFs). Regulation of Arp2/3 activity is achieved by endogenous inhibitory proteins through direct binding to Arp2/3 and competition with NPFs or by binding to Arp2/3-induced actin filaments and disassembly of branched actin networks. Arp2/3 inhibition has recently garnered more attention as it has been associated with attenuation of cancer progression, neurotoxic effects during drug abuse, and pathogen invasion of host cells. In this review, we summarize current knowledge on expression, inhibitory mechanisms and function of endogenous proteins able to inhibit Arp2/3 such as coronins, GMFs, PICK1, gadkin, and arpin. Moreover, we discuss cellular consequences of pharmacological Arp2/3 inhibition.
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