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Article

A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division.

The Journal of biological chemistry - 15 Oct 2010

Chang Chuang-Rung, Manlandro Cara Marie, Arnoult Damien, Stadler Julia, Posey Ammon E, Hill R Blake, Blackstone Craig

Abstract excerpt

Mitochondria dynamically fuse and divide within cells, and the proper balance of fusion and fission is necessary for normal mitochondrial function, morphology, and distribution. Drp1 is a dynamin-related GTPase required for mitochondrial fission in mammalian cells. It harbors four distinct domains: GTP-binding, middle, insert B, and GTPase effector. A lethal mutation (A395D) within the Drp1 middle domain was...

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Identifiers

PMID: 20696759
DOI: 10.1074/jbc.M110.142430
PMCID: PMC2952251

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Source receipt: pubmed, retrieved 7 Sept 2026.

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