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The gelsolin:calponin complex nucleates actin filaments with distinct morphologies |
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| Authors: | Imen Ferjani Abdellatif Fattoum Bastien Seantier Mohamed Manai Claude Roustan Sutherland K Maciver |
| Institution: | a DIMNP, University of Montpellier 2 and 1, CNRS Montpellier, Place E. Bataillon, CC107, 34095 Montpellier Cedex 5, France b Laboratoire de motilité cellulaire (Ecole Pratique des Hautes Etudes), Place E. Bataillon, CC107, 34095 Montpellier Cedex 5, France c Centre for Integrative Physiology, School of Biomedical Sciences, University of Edinburgh, Hugh Robson Building, George Square, Edinburgh EH8 9XD, UK d Centre de Recherches de Biochimie Macromoléculaire, UMR 5237 (CNRS), 1919 rte de Mende, 34293 Montpellier Cedex 5, France e Unité de Biochimie et Biologie Moléculaire, Faculté des Sciences de Tunis, Campus Universitaire 2092 El Manar, Tunis, Tunisia f INSERM, Unité 554, University of Montpellier 1 and 2, CNRS, UMR 5048, Centre de Biochimie Structurale, 29 rue de Navacelle, Montpellier, France |
| Abstract: | Gelsolin and calponin are cytoskeletal and signalling proteins that form a tight 1:1 complex (GCC). We show that calponin within the GCC inhibits the rate of gelsolin mediated nucleation of actin polymerization. The actin-binding function of calponin is ablated within the GCC as the actin-binding site overlaps with one of the gelsolin binding sites. The structure of filaments that result from nucleation by GCC are different to those nucleated by gelsolin alone in that they are longer, loosely bundled and stain heterogeneously with phalloidin. GCC nucleated filaments appear contorted and wrap around each to form the loose bundles. |
| Keywords: | CH calponin homology domain G1-6 the six repeated domains that comprise gelsolin |
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