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EMBO Rep. 2006 Oct;7(10):1019-22. Epub 2006 Aug 25.

MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology.

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Department of Biological Sciences, Tokyo Institute of Technology, 4259-B19 Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Japan.


Mitofusins and Drp1 are key components in mitochondrial membrane fusion and division, but the molecular mechanism underlying the regulation of their activities remains to be clarified. Here, we identified human membrane-associated RING-CH (MARCH)-V as a novel transmembrane protein of the mitochondrial outer membrane. Immunoprecipitation studies demonstrated that MARCH-V interacts with mitofusin 2 (MFN2) and ubiquitinated forms of Drp1. Overexpression of MARCH-V promoted the formation of long tubular mitochondria in a manner that depends on MFN2 activity. By contrast, mutations in the RING finger caused fragmentation of mitochondria. We also show that MARCH-V promotes ubiquitination of Drp1. These results indicate that MARCH-V has a crucial role in the control of mitochondrial morphology by regulating MFN2 and Drp1 activities.

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