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The N-terminal Ac-EEED sequence plays a role in alpha-smooth-muscle actin incorporation into stress fibersстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Clement S., Hinz B., Dugina V., Gabbiani G., Chaponnier C.
- Журнал: Journal of Cell Science
- Том: 118
- Номер: 7
- Год издания: 2005
- Издательство: The Company of Biologists Ltd.
- Местоположение издательства: United Kingdom
- Первая страница: 1395
- Последняя страница: 1404
- DOI: 10.1242/jcs.01732
- Аннотация: We have previously shown that the N-terminal sequence AcEEED of alpha-smooth-muscle actin causes the loss of alpha-smooth-muscle actin from stress fibers and a decrease in cell contractility when introduced in myofibroblasts as a cell-penetrating fusion peptide. Here, we have investigated the function of this sequence on stress fiber organization in living cells, using enhanced green fluorescent protein (EGFP)-tagged alpha-smooth-muscle actin. The fusion peptide provokes the gradual disappearance of EGFP fluorescence of (x-smooth-muscle actin from stress fibers and the formation of hitherto unknown rod-like structures. In addition to (x-smooth-muscle actin, these structures contain cytoplasmic actins, gelsolin and cofilin but not other major actin-binding proteins. These rod-like structures are also visible in wild-type fibroblasts during normal cell spreading, suggesting that they represent a physiological step in the organization of alpha-smooth-muscle actin in stress fibers. Fluorescence-recovery-after-photobleaching experiments suggest that the fusion peptide reduces the dynamics of alpha-smooth-muscle actin and its incorporation in stress fibers. Here, we propose a new mechanism of how alpha-smooth-muscle actin is incorporated in stress fibers involving the sequence Ac-EEED.
- Добавил в систему: Дугина Вера Борисовна