Mitochondrial Homeostasis: How Do Dimers of Mitofusins Mediate Mitochondrial Fusion?

Oliver Daumke; Aurélien Roux

doi:10.1016/j.cub.2017.03.024

Mitochondrial Homeostasis: How Do Dimers of Mitofusins Mediate Mitochondrial Fusion?

Curr Biol. 2017 May 8;27(9):R353-R356. doi: 10.1016/j.cub.2017.03.024.

Authors

Oliver Daumke¹, Aurélien Roux²

Affiliations

¹ Max-Delbrück Centrum für Molekulare Medizin, Crystallography Robert-Rössle-Strasse 10, 13125 Berlin, Germany; Freie Universität Berlin, Institute of Chemistry and Biochemistry, Takustraße 6, 14195 Berlin, Germany. Electronic address: oliver.daumke@mdc-berlin.de.
² University of Geneva, Department of Biochemistry, 30 quai Ernest Ansermet, CH-1211 Geneva 4, Switzerland; Swiss National Centre for Competence in Research Programme Chemical Biology, CH-1211 Geneva, Switzerland. Electronic address: aurelien.roux@unige.ch.

PMID: 28486121
DOI: 10.1016/j.cub.2017.03.024

Abstract

Mitochondria have high fusion and fission rates to maintain their size and number throughout the cell cycle. How is fusion mediated? New structural studies propose mechanisms by which the dynamin-like mitofusin proteins promote fusion of mitochondria.

MeSH terms

Homeostasis
Membrane Fusion*
Mitochondria / metabolism*
Mitochondrial Dynamics
Mitochondrial Membrane Transport Proteins / chemistry*
Mitochondrial Membrane Transport Proteins / metabolism
Mitochondrial Membranes / metabolism
Protein Multimerization

Substances

Mitochondrial Membrane Transport Proteins