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• W2897819932 abstract "Cellular actin assembly is controlled at the barbed ends of actin filaments, where capping protein (CP) limits polymerization. Twinfilin is a conserved in vivo binding partner of CP, yet the significance of this interaction has remained a mystery. Here, we discover that the C-terminal tail of Twinfilin harbors a CP-interacting (CPI) motif, identifying it as a novel CPI-motif protein. Twinfilin and the CPI-motif protein CARMIL have overlapping binding sites on CP. Further, Twinfilin binds competitively with CARMIL to CP, protecting CP from barbed-end displacement by CARMIL. Twinfilin also accelerates dissociation of the CP inhibitor V-1, restoring CP to an active capping state. Knockdowns of Twinfilin and CP each cause similar defects in cell morphology, and elevated Twinfilin expression rescues defects caused by CARMIL hyperactivity. Together, these observations define Twinfilin as the first ‘pro-capping’ ligand of CP and lead us to propose important revisions to our understanding of the CP regulatory cycle." @default.
• W2897819932 created "2018-10-26" @default.
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• W2897819932 date "2018-10-23" @default.
• W2897819932 modified "2023-09-26" @default.
• W2897819932 title "A novel mode of capping protein-regulation by twinfilin" @default.
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• W2897819932 doi "https://doi.org/10.7554/elife.41313" @default.
• W2897819932 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6249002" @default.
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