Nucleoside diphosphate kinases fuel dynamin superfamily proteins with GTP for membrane remodeling-Reference-Cited by-同舟云学术

Nucleoside diphosphate kinases fuel dynamin superfamily proteins with GTP for membrane remodeling

Published:2014-06-27 Issue:6191 Volume:344 Page:1510-1515
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Boissan Mathieu¹²³⁴,Montagnac Guillaume¹²,Shen Qinfang⁵,Griparic Lorena⁵,Guitton Jérôme⁶⁷,Romao Maryse¹⁸,Sauvonnet Nathalie⁹,Lagache Thibault¹⁰,Lascu Ioan¹¹,Raposo Graça¹⁸,Desbourdes Céline¹²¹³,Schlattner Uwe¹²¹³,Lacombe Marie-Lise³⁴,Polo Simona¹⁴¹⁵,van der Bliek Alexander M.⁵,Roux Aurélien¹⁶,Chavrier Philippe¹²

Affiliation:

1. Institut Curie, Research Center, Paris, France.

2. Membrane and Cytoskeleton Dynamics, CNRS UMR 144, Paris, France.

3. Université Pierre et Marie Curie, University Paris 06, Paris, France.

4. Saint-Antoine Research Center, INSERM UMR-S 938, Paris, France.

5. Department of Biological Chemistry, David Geffen School of Medicine at University of California, Los Angeles, Los Angeles, CA, USA.

6. Hospices Civils de Lyon, Pierre Bénite, France.

7. Université de Lyon, Lyon, France.

8. Structure and Membrane Compartments, CNRS UMR 144, Paris, France.

9. Institut Pasteur, Unité de Biologie des Interactions Cellulaires, Paris, France.

10. Quantitative Image Analysis Unit, Institut Pasteur, Paris, France.

11. Institut de Biochimie et Génétique Cellulaires-CNRS, Université Bordeaux 2, Bordeaux, France.

12. Université Grenoble Alpes, Laboratory of Fundamental and Applied Bioenergetics, Grenoble, France.

13. Inserm, U1055, Grenoble, France.

14. IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, Milan, Italy.

15. Dipartimento di Scienze della Salute, Universita’ degli Studi di Milano, Milan, Italy.

16. Biochemistry Department, University of Geneva, & Swiss National Center for Competence in Research Program Chemical Biology, Geneva, Switzerland.

Abstract

Supplying power: Right time, right place Cell membranes are very flexible and easily molded to shape; however, to physically pinch off a membrane vesicle from a membrane tube still requires power. A type of molecular machine known as dynamin is involved in this sort of membrane remodeling. Dynamins use guanosine triphosphate (GTP) rather than the more commonly used cellular energy source adenosine triphosphate to work. Boissan et al. now show that two separate dynamins found in the cytoplasm or the mitochondria both use the same sort of enzyme—nucleoside diphosphate kinases—to provide GTP at just the right time and the right place to power membrane fission. Science , this issue p. 1510

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference33 articles.

1. Dynamin, a membrane-remodelling GTPase

2. Dynamin: Functional Design of a Membrane Fission Catalyst

3. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding

4. Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals

5. Dynamin Undergoes a GTP-Dependent Conformational Change Causing Vesiculation

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