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. 2021 Jan 27;7(5):eabd5271. doi: 10.1126/sciadv.abd5271

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Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

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Fig. 6 — (A) Cartoon comparison of CP and CP/twinfilin association at the barbed end of a filament. (B) Twinfilin-aided uncapping is a result of twinfilin ADF-H domains inducing G-actin–like conformations in the terminal two actin protomers, weakening actin:actin interactions in the filament, leading to the dissociation of the complex. (C) Twinfilin/V-1–aided uncapping requires space for V-1 to reach its binding site on CP via a wobble state of the twinfilin-bound complex. Once V-1 is bound, CP is unable to reassociate with actin. In vitro effects of twinfilin alone on actin filaments and comparisons of uncapping models in the absence of twinfilin are shown in fig. S9.