| ID | 67607 |
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| Author |
Yamada, Hiroshi
Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
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Osaka, Hirona
Graduate School of Science, Nagoya University
Tatsumi, Nanami
Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Araki, Miu
Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Abe, Tadashi
Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Kaihara, Keiko
Department of Cardiovascular Physiology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Takahashi, Ken
Department of Cardiovascular Physiology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
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Takashima, Eizo
Division of Malaria Research, Proteo-Science Center, Ehime University
Uchihashi, Takayuki
Graduate School of Science, Nagoya University
Naruse, Keiji
Department of Cardiovascular Physiology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
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Takei, Kohji
Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
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| 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 a bundling of the actin filaments in the absence of alpha-actinin and enhanced the 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 fixed the movements of the two proteins on the actin filaments. These results strongly suggest that SYNPO2L cooperates with alpha-actinin during actin bundle formation to facilitate sarcomere formation and maintenance.
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| Keywords | SYNPO2L
actinin
actin
sarcomere
cardiomyocyte
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| Published Date | 2024-08-17
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| Publication Title |
Cells
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| Volume | volume13
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| Issue | issue16
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| Publisher | MDPI
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| Start Page | 1373
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| ISSN | 2073-4409
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| Content Type |
Journal Article
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| language |
English
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| OAI-PMH Set |
岡山大学
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| Copyright Holders | © 2024 by the authors.
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| File Version | publisher
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| PubMed ID | |
| DOI | |
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| Related Url | isVersionOf https://doi.org/10.3390/cells13161373
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| License | https://creativecommons.org/licenses/by/4.0/
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| Citation | Yamada, H.; Osaka, H.; Tatsumi, N.; Araki, M.; Abe, T.; Kaihara, K.; Takahashi, K.; Takashima, E.; Uchihashi, T.; Naruse, K.; et al. Direct Binding of Synaptopodin 2-Like Protein to Alpha-Actinin Contributes to Actin Bundle Formation in Cardiomyocytes. Cells 2024, 13, 1373. https://doi.org/10.3390/cells13161373
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| Funder Name |
Ministry of Education, Culture, Sports, Science and Technology
Okayama University Central Research Laboratory
Ehime University Proteo-Science Center (PROS)
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| 助成番号 | JP24K01309
JP23K27170
JP22K06580
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