AMP-activated protein kinase mediates mitochondrial fission in response to energy stress-Reference-Cited by-同舟云学术

AMP-activated protein kinase mediates mitochondrial fission in response to energy stress

Published:2016-01-15 Issue:6270 Volume:351 Page:275-281
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Toyama Erin Quan¹,Herzig Sébastien¹,Courchet Julien²,Lewis Tommy L.²,Losón Oliver C.³,Hellberg Kristina¹,Young Nathan P.¹,Chen Hsiuchen³,Polleux Franck²,Chan David C.³,Shaw Reuben J.¹

Affiliation:

1. Molecular and Cell Biology Laboratory and Howard Hughes Medical Institute, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.

2. Department of Neuroscience, Zuckerman Mind Brain Behavior Institute and Kavli Institute for Brain Science, Columbia University, New York, NY 10032, USA.

3. Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA.

Abstract

How to shape mitochondrial networks Mitochondria undergo fragmentation or fusion in response to changes in cellular metabolism. Toyama et al. report that adenosine monophosphate-activated protein kinase (AMPK) is both necessary and sufficient to control mitochondrial fragmentation. AMPK functions as a sensor to monitor the energy status of the cell by phosphorylating mitochondrial fission factor (MFF), a protein of the mitochondrial outer membrane. MFF then acts to recruit a cytoplasmic guanosine triphosphatase that promotes mitochondrial fission. Science , this issue p. 275

Funder

NIH

Leona M. and Harry B. Helmsley Charitable Trust

American Cancer Society

European Molecular Biology Organization (EMBO)

George E. Hewitt Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference40 articles.

1. Mitochondrial dynamics and inheritance during cell division, development and disease