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Myopathy-causing mutation R91P in the TPM3 gene drastically impairs structural and functional properties of slow skeletal muscle tropomyosin γβ-heterodimerстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 15 февраля 2024 г.
- Авторы: Gonchar Anastasiia D., Koubassova Natalia A., Kopylova Galina V., Kochurova Anastasia M., Nefedova Victoria V., Yampolskaya Daria S., Shchepkin Daniil V., Bershitsky Sergey Y., Tsaturyan Andrey K., Matyushenko Alexander M., Levitsky Dmitrii I.
- Журнал: Archives of Biochemistry and Biophysics
- Год издания: 2024
- Издательство: Academic Press
- Местоположение издательства: United States
- Номер статьи: 109881
- DOI: 10.1016/j.abb.2023.109881
- Аннотация: Tropomyosin (Tpm) is a regulatory actin-binding protein involved in Ca2+ activation of contraction of striated muscle. In human slow skeletal muscles, two distinct Tpm isoforms, γ and β, are present. They interact to form three types of dimeric Tpm molecules: γγ-homodimers, γβ-heterodimers, or ββ-homodimers, and a majority of the molecules are present as γβ-Tpm heterodimers. Point mutation R91P within the TPM3 gene encoding γ-Tpm is linked to the condition known as congenital fiber-type disproportion (CFTD), which is characterized by severe muscle weakness. Here, we investigated the influence of the R91P mutation in the γ-chain on the properties of the γβ-Tpm heterodimer. We found that the R91P mutation impairs the functional properties of γβ-Tpm heterodimer more severely than those of earlier studied γγ-Tpm homodimer carrying this mutation in both γ-chains. Since a significant part of Tpm molecules in slow skeletal muscle is present as γβ-heterodimers, our results explain why this mutation leads to muscle weakness in CFTD.
- Добавил в систему: Кубасова Наталия Алексеевна