AI Article Synopsis
- * The study shows that ASAP1 directly regulates actin filament assembly through its specific domains, particularly the BAR-PH segment, which helps bundle the filaments.
- * Depleting ASAP1 leads to disorganized stress fibers, while increasing its levels enhances actin remodeling, indicating that ASAP1 plays a critical role in maintaining the cell's cytoskeletal integrity.
Article Abstract
ASAP1 is a multi-domain ArfGAP that controls cell migration, spreading, and focal adhesion dynamics. Although its GAP activity contributes to remodeling of the actin cytoskeleton, it does not fully explain all cellular functions of ASAP1. Here we find that ASAP1 regulates actin filament assembly directly through its N-BAR domain and controls stress fiber maintenance. ASAP1 depletion caused defects in stress fiber organization. Conversely, overexpression of ASAP1 enhanced actin remodeling. The BAR-PH fragment was sufficient to affect actin. ASAP1 with the BAR domain replaced with the BAR domain of the related ACAP1 did not affect actin. The BAR-PH tandem of ASAP1 bound and bundled actin filaments directly, whereas the presence of the ArfGAP and the C-terminal linker/SH3 domain reduced binding and bundling of filaments by BAR-PH. Together these data provide evidence that ASAP1 may regulate the actin cytoskeleton through direct interaction of the BAR-PH domain with actin filaments.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6889188 | PMC |
| http://dx.doi.org/10.1016/j.isci.2019.11.015 | DOI Listing |
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