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. 2019 Aug 29;9:12580. doi: 10.1038/s41598-019-48884-w

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© The Author(s) 2019

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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Identification of four amino acids located in the domain unique to the cardiac isoform required for interacting with α-actinin2. (A) Schematics of cMLCK protein including four amino acids 171–174 at the N-terminus region specific for cardiac isoform. (B) Two N-terminus deletion mutants, HA-tagged cMLCK(171–795) and cMLCK(175–795), were mixed with Myc-tagged full-length α-actinin2. Presence ( + ) and absence (−) of interaction between two proteins were indicated. (C) Internal deletion mutant of cMLCK (Δ171–174), and (D) four amino acid substituted mutants from ¹⁷¹DVKP¹⁷⁴ to ¹⁷¹AAAA¹⁷⁴ were mixed with Myc-tagged full-length α-actinin2. (E) Schematics of α-actinin2 protein including the second actin binding site. (F) Two Myc-tagged N-terminus deletion mutants of α-actinin2 with or without ABS2 domain were mixed with HA-full-length cMLCK. The additional results were available in Supplemental Fig. 1. ABS, F-actin binding site; SR, spectrin repeat; EF, EF hand motif.