The Arf GTPase-activating Protein, ASAP1, Binds Nonmuscle Myosin 2A to Control Remodeling of the Actomyosin Network

J Biol Chem. 2016 Apr 1;291(14):7517-26. doi: 10.1074/jbc.M115.701292. Epub 2016 Feb 17.


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.

Keywords: ADP ribosylation factor (ARF); GTPase-activating protein (GAP); actin; cell biology; cell migration; cytoskeleton; myosin.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Actomyosin / genetics
  • Actomyosin / metabolism*
  • Adaptor Proteins, Signal Transducing / genetics
  • Adaptor Proteins, Signal Transducing / metabolism*
  • Animals
  • Cell Movement / physiology*
  • HeLa Cells
  • Humans
  • Mice
  • NIH 3T3 Cells
  • Nonmuscle Myosin Type IIA / genetics
  • Nonmuscle Myosin Type IIA / metabolism*
  • Protein Binding
  • Protein Structure, Tertiary
  • Signal Transduction / physiology*


  • ASAP1 protein, human
  • Adaptor Proteins, Signal Transducing
  • Asap1 protein, mouse
  • Actomyosin
  • Nonmuscle Myosin Type IIA