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JCS ePress
online publication date 15 Mar 2005
doi: 10.1242/jcs.01732
Research Article
The N-terminal Ac-EEED sequence plays a role in 
-smooth-muscle actin incorporation into stress fibers
Sophie Clément,
Boris Hinz,
Vera Dugina,
Giulio Gabbiani,
and
Christine Chaponnier*
* Author for correspondence (e-mail: christine.chaponnier{at}medecine.unige.ch)
We have previously shown that the N-terminal sequence AcEEED of 
-smooth-muscle actin causes the loss of -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 -smooth-muscle actin. The fusion peptide provokes the gradual disappearance of EGFP fluorescence of -smooth-muscle actin from stress fibers and the formation of hitherto unknown rod-like structures. In addition to -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 -smooth-muscle actin in stress fibers. Fluorescence-recovery-after-photobleaching experiments suggest that the fusion peptide reduces the dynamics of -smooth-muscle actin and its incorporation in stress fibers. Here, we propose a new mechanism of how -smooth-muscle actin is incorporated in stress fibers involving the sequence Ac-EEED.
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