1. Architecture Dependence of Actin Filament Network Disassembly
- Author
-
Christophe Guérin, Laurent Blanchoin, Audrey Guillotin, Laurène Gressin, Alphée Michelot, Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), ANR-10- LABX-49-01,Labex GRAL,Labex GRAL, ANR-12-BSV5-0014,Contract,Nouveaux systèmes biomimétiques pour étudier la contractilité acto-myosine cellulaire(2012), ANR-14-CE11-0011-01,DiANe,ANR-14-CE11-0011-01, Irtelis PhD fellowship (CEA), Labex GRAL, ANR (ANR-12-BSV5-0014, ANR-14-CE11-0011-01), ANR-10-LABX-0049,GRAL,Grenoble Alliance for Integrated Structural Cell Biology(2010), ANR-14-CE11-0011,Diane,Contractilité de réseaux d'actine induite par leur désassemblage(2014), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)
- Subjects
[SDV.BC]Life Sciences [q-bio]/Cellular Biology ,macromolecular substances ,Biology ,environment and public health ,General Biochemistry, Genetics and Molecular Biology ,Protein filament ,03 medical and health sciences ,0302 clinical medicine ,Yeasts ,Filament severing ,Animals ,actin network ,Cytoskeleton ,Actin ,030304 developmental biology ,0303 health sciences ,Aip1 ,Agricultural and Biological Sciences(all) ,Biochemistry, Genetics and Molecular Biology(all) ,Microfilament Proteins ,Actin remodeling ,Microfilament Protein ,Cofilin ,Actin cytoskeleton ,Actins ,Cell biology ,Actin Cytoskeleton ,Actin Depolymerizing Factors ,Rabbits ,MDia1 ,ADF/Cofilin ,General Agricultural and Biological Sciences ,030217 neurology & neurosurgery - Abstract
International audience; Turnover of actin networks in cells requires the fast disassembly of aging actin structures. While ADF/cofilin and Aip1 have been identified as central players, how their activities are modulated by the architecture of the networks remains unknown. Using our ability to reconstitute a diverse array of cellular actin organizations, we found that ADF/cofilin binding and ADF/cofilin-mediated disassembly both depend on actin geometrical organization. ADF/cofilin decorates strongly and stabilizes actin cables, whereas its weaker interaction to Arp2/3 complex networks is correlated with their dismantling and their reorganization into stable architectures. Cooperation of ADF/cofilin with Aip1 is necessary to trigger the full disassembly of all actin filament networks. Additional experiments performed at the single-molecule level indicate that this cooperation is optimal above a threshold of 23 molecules of ADF/cofilin bound as clusters along an actin filament. Our results indicate that although ADF/cofilin is able to dismantle selectively branched networks through severing and debranching, stochastic disassembly of actin filaments by ADF/cofilin and Aip1 represents an efficient alternative pathway for the full disassembly of all actin networks. Our data support a model in which the binding of ADF/cofilin is required to trigger a structural change of the actin filaments, as a prerequisite for their disassembly by Aip1.
- Published
- 2015
- Full Text
- View/download PDF