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• W2989355358 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." @default.
• W2989355358 created "2019-11-22" @default.
• W2989355358 creator A5004574231 @default.
• W2989355358 creator A5008383835 @default.
• W2989355358 creator A5050751520 @default.
• W2989355358 creator A5061371289 @default.
• W2989355358 creator A5076063652 @default.
• W2989355358 date "2019-12-01" @default.
• W2989355358 modified "2023-10-15" @default.
• W2989355358 title "The ArfGAP ASAP1 Controls Actin Stress Fiber Organization via Its N-BAR Domain" @default.
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• W2989355358 doi "https://doi.org/10.1016/j.isci.2019.11.015" @default.
• W2989355358 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6889188" @default.
• W2989355358 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31785555" @default.
• W2989355358 hasPublicationYear "2019" @default.
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