Reference: Naylor K, et al. (2006) Mdv1 interacts with assembled dnm1 to promote mitochondrial division. J Biol Chem 281(4):2177-83

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Abstract


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.

Reference Type
Journal Article | Research Support, N.I.H., Extramural
Authors
Naylor K, Ingerman E, Okreglak V, Marino M, Hinshaw JE, Nunnari J
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