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Article

Mdv1 interacts with assembled dnm1 to promote mitochondrial division.

The Journal of biological chemistry - 27 Jan 2006

Naylor Kari, Ingerman Elena, Okreglak Voytek, Marino Michael, Hinshaw Jenny E, Nunnari Jodi

Abstract excerpt

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...

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Identifiers

PMID: 16272155
DOI: 10.1074/jbc.M507943200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Click a neighbor to travelStep 1 · 12 closest

Mdv1 interacts with assembled dnm1 to promote mitochondrial division.PMID 16272155Read ↗

Mdv1p Is a Wd Repeat Protein That Interacts with the Dynamin-Related Gtpase, Dnm1p, to Trigger Mitochondrial DivisionSemantic proximity Read ↗

Dnm1 forms spirals that are structurally tailored to fit mitochondria.Semantic proximity Read ↗

The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria.Semantic proximity Read ↗

The GTPase effector domain sequence of the Dnm1p GTPase regulates self-assembly and controls a rate-limiting step in mitochondrial fission.Semantic proximity Read ↗

The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly.Semantic proximity Read ↗

Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells.Semantic proximity Read ↗

Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p.Semantic proximity Read ↗

Division of mitochondria requires a novel DNM1-interacting protein, Net2p.Semantic proximity Read ↗

Structural basis for recruitment of mitochondrial fission complexes by Fis1.Semantic proximity Read ↗

Structural Basis for Regulated Assembly of the Mitochondrial Fission GTPase Drp1Semantic proximity Read ↗

Intra- and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1.Semantic proximity Read ↗

Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1.Semantic proximity Read ↗

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