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J. Biol. Chem., Vol. 281, Issue 4, 2177-2183, January 27, 2006

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Mdv1 Interacts with Assembled Dnm1 to Promote Mitochondrial Division^*

Kari Naylor, Elena Ingerman, Voytek Okreglak1, Michael Marino, Jenny E. Hinshaw, and Jodi Nunnari2

From the Section of Molecular and Cellular Biology, University of California, Davis, California 95616 and the Laboratory of Cell Biochemistry and Biology, National Institutes of Health, NIDDK, Bethesda, Maryland 20892

The dynamin-related GTPase, Dnm1, self-assembles into punctate structures that are targeted to the outer mitochondrial membrane where they mediate mitochondrial division. Post-targeting, Dnm1-dependent division is controlled by the actions of the WD repeat protein, Mdv1, and the mitochondrial tetratricopeptide repeat-like outer membrane protein, Fis1. Our previous studies suggest a model where at this step Mdv1 functions as an adaptor linking Fis1 with Dnm1. To gain insight into the exact role of the Fis1·Mdv1·Dnm1 complex in mitochondrial division, we performed a structure-function analysis of the Mdv1 adaptor. Our analysis suggests that dynamic interactions between Mdv1 and Dnm1 play a key role in division by regulating Dnm1 self-assembly.

Received for publication, July 21, 2005 , and in revised form, October 5, 2005.

^* This work was supported by National Institutes of Health Grants 1R01EY015924 and 5R01GM062942 (to J. N.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Movie 1.

¹ Present address: Section of Molecular and Cellular Biology, University of California, Berkeley, CA.

² To whom correspondence should be addressed. Tel.: 530-754-9774; Fax: 530-752-7522; E-mail: jmnunnari{at}ucdavis.edu.

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