Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The Journal of biological chemistry - 23 Jun 2006

Bhar Debjani, Karren Mary Anne, Babst Markus, Shaw Janet M

Abstract excerpt

Interactions between yeast Dnm1p, Mdv1p, and Fis1p are required to form fission complexes that catalyze division of the mitochondrial compartment. During the formation of mitochondrial fission complexes, the Dnm1p GTPase self-assembles into large multimeric complexes on the outer mitochondrial me...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adaptor Proteins, Signal Transducing
Share to Cytoplasm
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Fungal

Share to GTP Phosphohydrolases

Share to Mitochondria

Share to Mitochondrial Proteins

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

PMID: 16601120
DOI: 10.1074/jbc.M513530200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16601120-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1.PMID 16601120Read ↗

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

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

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

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

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

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

The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mitochondria.Semantic proximity Read ↗

Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane.Semantic proximity Read ↗

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

Phospholipid association is essential for dynamin-related protein Mgm1 to function in mitochondrial membrane fusion.Semantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.