Direct Binding of Synaptopodin 2-Like Protein to Alpha-Actinin Contributes to Actin Bundle Formation in Cardiomyocytes
Authors:
- Hiroshi YamadaHYHiroshi Yamada
- Hirona OsakaHOHirona Osaka
- Nanami TatsumiNTNanami Tatsumi
- Miu ArakiMAMiu Araki
- Tadashi AbeTATadashi Abe
- Keiko KaiharaKKKeiko Kaihara
- Ken TakahashiKen Takahashi
- Eizo TakashimaETEizo Takashima
- Takayuki UchihashiTUTakayuki Uchihashi
- Keiji NaruseKNKeiji Naruse
- Kohji TakeiKTKohji Takei
Preprint
- 29 July 2024
- preprint
- Published by MDPI AG in Preprints.org
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 alpha-actinin and actin filaments in cultured mouse cardiomyocytes. Immunofluorescence studies showed that SYNPO2L colocalized with alpha-actinin and actin filaments at the Z-discs of the sarcomere. Recombinant SYNPO2La or SYNPO2Lb caused bundling of actin filaments in the absence of alpha-actinin and enhanced alpha-actinin-dependent formation of actin bundles. In addition, high-speed atomic force microscopy revealed that SYNPO2La directly bound to alpha-actinin via its globular ends. The interaction between alpha-actinin and SYNPO2La stabilized the two proteins on actin filaments. These results strongly suggest that SYNPO2L cooperates with alpha-actinin during actin bundle formation to facilitate sarcomere formation and maintenance.Keywords
All Related Versions
- Version 1, 2024-07-29, Preprints
- Published version: Cells, 13 (16), 1373.