Key result
ASAP1 directly binds nonmuscle myosin 2A (NM2A) via its BAR domain, acting as a positive regulator of NM2A to control remodeling of the actomyosin network, cell spreading, and migration.
ASAP1 directly binds and positively regulates NM2A, linking signaling to the mechanical machinery of cell migration.
ASAP1 regulates F-actin-based structures and functions, including focal adhesions (FAs) and circular dorsal ruffles (CDRs), cell spreading and migration. ASAP1 function requires its N-terminal BAR domain. We discovered that nonmuscle myosin 2A (NM2A) directly bound the BAR-PH tandem of ASAP1in vitro ASAP1 and NM2A co-immunoprecipitated and colocalized in cells. Knockdown of ASAP1 reduced colocalization of NM2A and F-actin in cells. Knockdown of ASAP1 or NM2A recapitulated each other's effects on FAs, cell migration, cell spreading, and CDRs. The NM2A-interacting BAR domain contributed to ASAP1 control of cell spreading and CDRs. Exogenous expression of NM2A rescued the effect of ASAP1 knockdown on CDRs but ASAP1 did not rescue NM2A knockdown defect in CDRs. Our results support the hypothesis that ASAP1 is a positive regulator of NM2A. Given other binding partners of ASAP1, ASAP1 may directly link signaling and the mechanical machinery of cell migration.
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Chen et al. (2016) studied this question. ASAP1 and NM2A knockdown was evaluated on Colocalization of NM2A and F-actin, focal adhesions, cell migration, cell spreading, and circular dorsal ruffles. ASAP1 directly binds nonmuscle myosin 2A (NM2A) via its BAR domain, acting as a positive regulator of NM2A to control remodeling of the actomyosin network, cell spreading, and migration.
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