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First published online 15 March 2005
doi: 10.1242/jcs.01732

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The N-terminal Ac-EEED sequence plays a role in -smooth-muscle actin incorporation into stress fibers

Sophie Clément^1,*, Boris Hinz^2,*, Vera Dugina³, Giulio Gabbiani¹ and Christine Chaponnier^1,

¹ Dept of Pathology and Immunology, CMU, Geneva, Switzerland
² Laboratory of Cell Biophysics, Ecole polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland
³ Moscow State University, 119899 Moscow, Russia

Author for correspondence (e-mail: christine.chaponnier{at}medecine.unige.ch)

Accepted 21 December 2004

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.

Key words: Actin isoforms, GFP fusion protein, Actin dynamism, Cytoskeleton, Actin-binding protein

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