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An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sitesстатья
Информация о цитировании статьи получена из
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Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 4 марта 2022 г.
- Авторы: Fedechkin Stanislav O., Brockerman Jacob, Luna Elizabeth J., Lobanov Michail Yu, Galzitskaya Oxana V., Smirnov Serge L.
- Журнал: Journal of Biomolecular Structure and Dynamics
- Том: 31
- Номер: 10
- Год издания: 2013
- Издательство: Adenine Press
- Местоположение издательства: United States
- Первая страница: 1150
- Последняя страница: 1159
- DOI: 10.1080/07391102.2012.726531
- Аннотация: Supervillin, the largest member of the villin/gelsolin family, is a cytoskeleton regulating, peripheral membrane protein. Supervillin increases cell motility and promotes invasive activity in tumors. Major cytoskeletal interactors, including filamentous actin and myosin II, bind within the unique supervillin amino terminus, amino acids 1-830. The structural features of this key region of the supervillin polypeptide are unknown. Here, we utilize circular dichroism and bioinformatics sequence analysis to demonstrate that the N-terminal part of supervillin forms an extended intrinsically disordered region (IDR). Our combined data indicate that the N-terminus of human and bovine supervillin sequences (positions 1-830) represents an IDR, which is the largest IDR known to date in the villin/gelsolin family. Moreover, this result suggests a potentially novel mechanism of regulation of myosin II and F-actin via the intrinsically disordered N-terminal region of hub protein supervillin.
- Добавил в систему: Галзитская Оксана Валериановна