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ID 67607
フルテキストURL
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著者
Yamada, Hiroshi Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University Kaken ID publons researchmap
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 ORCID Kaken ID publons researchmap
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 ORCID Kaken ID publons researchmap
Takei, Kohji Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University Kaken ID publons researchmap
抄録
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.
キーワード
SYNPO2L
actinin
actin
sarcomere
cardiomyocyte
発行日
2024-08-17
出版物タイトル
Cells
13巻
16号
出版者
MDPI
開始ページ
1373
ISSN
2073-4409
資料タイプ
学術雑誌論文
言語
英語
OAI-PMH Set
岡山大学
著作権者
© 2024 by the authors.
論文のバージョン
publisher
PubMed ID
DOI
Web of Science KeyUT
関連URL
isVersionOf https://doi.org/10.3390/cells13161373
ライセンス
https://creativecommons.org/licenses/by/4.0/
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
助成機関名
Ministry of Education, Culture, Sports, Science and Technology
Okayama University Central Research Laboratory
Ehime University Proteo-Science Center (PROS)
助成番号
JP24K01309
JP23K27170
JP22K06580