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. 2021 Sep 9;12:5329. doi: 10.1038/s41467-021-25682-5

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 7 — Top panel: Actin monomers compete with free barbed ends for NPF WH2 binding. Binding of the former generates the nucleation-competent NPF state (1), whereas binding of the latter sequesters the NPF in an inactive configuration (2). Binding of wildtype capping protein masks the terminal subunits preventing NPF interaction, thereby indirectly stimulating nucleation. Bottom panel: Deletion of the β tentacle unmasks the terminal actin protomer, allowing capped ends to tether additional NPF proteins in an inactive state (3). This strengthens the tethering between actin network and the membrane and decreases the nucleation rate and network growth velocity.