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

Published in Journal of Cell Science. 2005, vol. 118, no. Pt 7, p. 1395-1404
Abstract 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 alpha-smooth-muscle actin from stress fibers and the formation of hitherto unknown rod-like structures. In addition to alpha-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.
Keywords Actins/drug effects/ physiology/ultrastructureAmino Acid SequenceAnimalsCell LineCell Movement/physiologyFibroblasts/drug effects/metabolism/ultrastructureFluorescence Recovery After PhotobleachingGreen Fluorescent Proteins/geneticsMolecular Sequence DataOligopeptides/pharmacology/ physiologyPeptide Fragments/pharmacologyProtein BindingRatsRecombinant Fusion Proteins/genetics/metabolismStress Fibers/drug effects/ physiology/ultrastructureTime Factors
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PMID: 15769852
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