Actin Binding to the BAR Domain and Arf GAP Activity of ASAP1 Coordinately Control Actin Stress Fibers and Focal Adhesions.

ABSTRACT:

Background

Actin stress fibers (SFs) and focal adhesions (FAs) are dynamic structures crucial to a range of cell behaviors including cell morphology, cell migration, proliferation, survival, and differentiation. The Arf GAP ASAP1 affects both SFs and FAs. Here, we test the hypothesis that two domains with distinct biochemical activities in ASAP1, the BAR domain that binds actin and nonmuscle myosin 2 (NM2) and the Arf GAP domain, which is necessary for inducing hydrolysis of GTP bound to Arf, coordinately regulate the structures.

Results

We found that ASAP1 associated with bundled actin, including SFs, colocalizing with α-actinin and nonmuscle myosin 2A (NM2A), and with paxillin in FAs. Reducing ASAP1 expression altered both SFs and FAs in four cell lines that we examined. T

SUBMITTER: Yoon HY 

PROVIDER: S-EPMC11975550 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature