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Membrane fission by dynamin: what we know and what we need to know.
Antonny, Bruno; Burd, Christopher; De Camilli, Pietro; Chen, Elizabeth; Daumke, Oliver; Faelber, Katja; Ford, Marijn; Frolov, Vadim A; Frost, Adam; Hinshaw, Jenny E; Kirchhausen, Tom; Kozlov, Michael M; Lenz, Martin; Low, Harry H; McMahon, Harvey; Merrifield, Christien; Pollard, Thomas D; Robinson, Phillip J; Roux, Aurélien; Schmid, Sandra.
Afiliación
  • Antonny B; CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis, Valbonne, France.
  • Burd C; Department of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
  • De Camilli P; Departments of Neuroscience and Cell Biology, Howard Hughes Medical Institute and Kavli Institute for Neuroscience, Yale University School of Medicine, New Haven, CT, USA.
  • Chen E; Department of Molecular Biology, UT Southwestern Medical Center, Dallas, TX, USA.
  • Daumke O; Department of Crystallography, Max-Delbrück Centrum für Molekulare Medizin, Berlin, Germany.
  • Faelber K; Department of Crystallography, Max-Delbrück Centrum für Molekulare Medizin, Berlin, Germany.
  • Ford M; Department of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
  • Frolov VA; Biofisika Institute (CSIC, UPV/EHU) and Department of Biochemistry and Molecular Biology, University of the Basque Country, Leioa, Spain.
  • Frost A; IKERBASQUE, Basque Foundation for Science, Bilbao, Spain.
  • Hinshaw JE; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA.
  • Kirchhausen T; Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD, USA.
  • Kozlov MM; Departments of Cell Biology and Pediatrics, Harvard Medical School, Boston, MA, USA.
  • Lenz M; Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.
  • Low HH; Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel.
  • McMahon H; LPTMS, CNRS, Univ. Paris-Sud, Université Paris-Saclay, Orsay, France.
  • Merrifield C; Department of Life Sciences, Imperial College, London, UK.
  • Pollard TD; MRC Laboratory of Molecular Biology, Cambridge, UK.
  • Robinson PJ; Institute for Integrative Biology of the Cell, Gif sur Yvette Cedex, France.
  • Roux A; Department of Molecular Cellular and Developmental Biology, Yale University, New Haven, CT, USA.
  • Schmid S; Cell Signalling Unit, Children's Medical Research Institute, The University of Sydney, Westmead, NSW, Australia.
EMBO J ; 35(21): 2270-2284, 2016 11 02.
Article en En | MEDLINE | ID: mdl-27670760
ABSTRACT
The large GTPase dynamin is the first protein shown to catalyze membrane fission. Dynamin and its related proteins are essential to many cell functions, from endocytosis to organelle division and fusion, and it plays a critical role in many physiological functions such as synaptic transmission and muscle contraction. Research of the past three decades has focused on understanding how dynamin works. In this review, we present the basis for an emerging consensus on how dynamin functions. Three properties of dynamin are strongly supported by experimental data first, dynamin oligomerizes into a helical polymer; second, dynamin oligomer constricts in the presence of GTP; and third, dynamin catalyzes membrane fission upon GTP hydrolysis. We present the two current models for fission, essentially diverging in how GTP energy is spent. We further discuss how future research might solve the remaining open questions presently under discussion.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Membrana Celular / Dinaminas Límite: Animals / Humans Idioma: En Revista: EMBO J Año: 2016 Tipo del documento: Article País de afiliación: Francia

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Membrana Celular / Dinaminas Límite: Animals / Humans Idioma: En Revista: EMBO J Año: 2016 Tipo del documento: Article País de afiliación: Francia