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. 2018 Apr 3;8:5503. doi: 10.1038/s41598-018-23816-2

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© The Author(s) 2018

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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TAGLN2-polymerized F-T/actin complex is resistant to depolymerization and has no preference between ATP-actin and ADP-actin. (a) Actin polymerization reactions containing actin and TAGLN2 (actin + TAGLN2) or actin alone (actin) in G-buffer and actin and TAGLN2 (actin + TAGLN2) or actin and phalloidin (actin + phalloidin) in F-buffer were diluted fivefold with G-buffer to initiate depolymerization in the absence (left) or presence (right) of cofilin. Results are representative of at least three independent experiments. (b) TAGLN2 uses both ATP-actin and ADP-actin for polymerization in G-buffer as monitored by fluorescence (left) or co-sedimentation (right). Results are representative of at least three independent experiments. Full-length blots/gels are presented in Supplementary Fig. S6.