Cellular morphology, adhesion, and motility occur through dynamic reorganization of actin-based superstructures. Actin-binding proteins are critical for regulating actin polymerization and superstructure formation. The Arp2/3 complex is an actin polymerization-inducing complex that includes Arp2, Arp3, p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc. Several nucleation promoting factors, such as WASP and coronin, regulate the activity of the Arp2/3 complex. In addition, the Arp2/3 complex may be regulated by phosphorylation of specific subunits in the complex. The p41-Arc (Arpc1) subunit has two isoforms in humans, Arpc1a and Arpc1b. PAK1 can bind and phosphorylate Thr-21 in Arpc1b leading to growth factor-stimulated cell motility. In addition, Arpc1b colocalizes with γ-tubulin at centrosomes and stimulates Aurora A activity. Aurora A phosphorylates Arpc1b on Thr-21 and a nonphosphorylatable Arpc1b mutant cannot activate Aurora A kinase and centrosome amplification. Thus, Arpc1b has roles in cytoskeletal dynamics during cell motility and mitosis, and these activities are regulated by phosphorylation at Thr-21.
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Vadlamudi, R.K. et al. (2004) EMBO Rep. 5(2):154.
Welch, M.D. et al. (1997) J Cell Biol. 138(2):375.
*For more information, see UniProt Accession O15143
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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