The gelsolin:calponin complex nucleates actin filaments with distinct morphologies
| Autor: | Bastien Seantier, Imen Ferjani, Abdellatif Fattoum, Mohamed Manai, Pierre-Emmanuel Milhiet, Nadir Bettache, Claude Roustan, Yves Benyamin, Sutherland K. Maciver |
|---|---|
| Přispěvatelé: | Dynamique des interactions membranaires normales et pathologiques (DIMNP), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Unité de Biochimie et Biologie Moléculaire, Faculté des Sciences Mathématiques, Physiques et Naturelles de Tunis (FST), Université de Tunis El Manar (UTM)-Université de Tunis El Manar (UTM), Centre de recherche en Biologie Cellulaire (CRBM), Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1), Centre de Biochimie Structurale [Montpellier] (CBS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre for Integrative Physiology, University of Edinburgh |
| Rok vydání: | 2009 |
| Předmět: |
Phalloidin
Calponin Biophysics Arp2/3 complex macromolecular substances MESH: Calcium-Binding Proteins MESH: Microscopy Electron Biochemistry 03 medical and health sciences chemistry.chemical_compound MESH: Microfilament Proteins Humans [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Binding site MESH: Microfilaments Cytoskeleton Molecular Biology Actin Gelsolin 030304 developmental biology 0303 health sciences MESH: Humans biology Chemistry 030302 biochemistry & molecular biology Calcium-Binding Proteins Microfilament Proteins Actin remodeling Cell Biology musculoskeletal system Cell biology Actin Cytoskeleton Microscopy Electron MESH: Gelsolin biology.protein |
| Zdroj: | Biochemical and Biophysical Research Communications Biochemical and Biophysical Research Communications, Elsevier, 2010, 392 (2), pp.118-23. ⟨10.1016/j.bbrc.2009.12.103⟩ |
| ISSN: | 1090-2104 0006-291X |
| DOI: | 10.1016/j.bbrc.2009.12.103⟩ |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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