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Article

The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly.

The Journal of cell biology - 24 Oct 2005

Karren Mary Anne, Coonrod Emily M, Anderson Teresa K, Shaw Janet M

Abstract excerpt

Mitochondrial division requires coordinated interactions among Fis1p, Mdv1p, and the Dnm1p GTPase, which assemble into fission complexes on the outer mitochondrial membrane. The integral outer membrane protein Fis1p contains a cytoplasmic domain consisting of a tetratricopeptide repeat (TPR)-like fold and a short NH(2)-terminal helix. Although it is known that the cytoplasmic domain is necessary for assembly of...

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Identifiers

PMID: 16247028
DOI: 10.1083/jcb.200506158
PMCID: PMC2171191

Genes

TPR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly.PMID 16247028Read ↗

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The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle.Semantic proximity Read ↗

Mdv1 interacts with assembled dnm1 to promote mitochondrial division.Semantic proximity Read ↗

Novel structure of the N terminus in yeast Fis1 correlates with a specialized function in mitochondrial fission.Semantic proximity Read ↗

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

Mutations in Fis1 disrupt orderly disposal of defective mitochondriaSemantic proximity Read ↗

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

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