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肌联蛋白 2 样蛋白与α-辅肌动蛋白的直接结合有助于心肌细胞中肌动蛋白束的形成。

Direct Binding of Synaptopodin 2-Like Protein to Alpha-Actinin Contributes to Actin Bundle Formation in Cardiomyocytes.

机构信息

Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, 2-5-1 Shikata-cho, Okayama 700-8558, Japan.

Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.

出版信息

Cells. 2024 Aug 17;13(16):1373. doi: 10.3390/cells13161373.

DOI:10.3390/cells13161373
PMID:39195263
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11352367/
Abstract

Synaptopodin 2-like protein (SYNPO2L) is localized in the sarcomere of cardiomyocytes and is involved in heart morphogenesis. However, the molecular function of SYNPO2L in the heart is not fully understood. We investigated the interaction of SYNPO2L with sarcomeric α-actinin and actin filaments in cultured mouse cardiomyocytes. Immunofluorescence studies showed that SYNPO2L colocalized with α-actinin and actin filaments at the Z-discs of the sarcomere. Recombinant SYNPO2La or SYNPO2Lb caused a bundling of the actin filaments in the absence of α-actinin and enhanced the α-actinin-dependent formation of actin bundles. In addition, high-speed atomic force microscopy revealed that SYNPO2La directly bound to α-actinin via its globular ends. The interaction between α-actinin and SYNPO2La fixed the movements of the two proteins on the actin filaments. These results strongly suggest that SYNPO2L cooperates with α-actinin during actin bundle formation to facilitate sarcomere formation and maintenance.

摘要

突触足蛋白 2 样蛋白（SYNPO2L）定位于心肌细胞的肌节中，参与心脏形态发生。然而，SYNPO2L 在心脏中的分子功能尚不完全清楚。我们研究了 SYNPO2L 在培养的小鼠心肌细胞中与肌节的α-辅肌动蛋白和肌动蛋白丝的相互作用。免疫荧光研究表明，SYNPO2L 与 α-辅肌动蛋白和肌动蛋白丝在肌节的 Z 盘处共定位。重组 SYNPO2La 或 SYNPO2Lb 在没有 α-辅肌动蛋白的情况下引起肌动蛋白丝的束状排列，并增强了 α-辅肌动蛋白依赖性的肌动蛋白束形成。此外，高速原子力显微镜显示 SYNPO2La 通过其球状末端直接与 α-辅肌动蛋白结合。α-辅肌动蛋白和 SYNPO2La 之间的相互作用固定了这两种蛋白在肌动蛋白丝上的运动。这些结果强烈表明，SYNPO2L 在肌动蛋白束形成过程中与 α-辅肌动蛋白协同作用，促进肌节的形成和维持。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/2c8ddfb8c42b/cells-13-01373-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/d0be0a18727b/cells-13-01373-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/dd71c8aa2c60/cells-13-01373-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/2fb6030a359d/cells-13-01373-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/3dbd8d524bdc/cells-13-01373-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/2c8ddfb8c42b/cells-13-01373-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/d0be0a18727b/cells-13-01373-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/dd71c8aa2c60/cells-13-01373-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/2fb6030a359d/cells-13-01373-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/3dbd8d524bdc/cells-13-01373-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ee73/11352367/2c8ddfb8c42b/cells-13-01373-g005.jpg

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