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

Dnm1 forms spirals that are structurally tailored to fit mitochondria.

The Journal of cell biology - 26 Sept 2005

Ingerman Elena, Perkins Edward M, Marino Michael, Mears Jason A, McCaffery J Michael, Hinshaw Jenny E, Nunnari Jodi

Abstract excerpt

Dynamin-related proteins (DRPs) are large self-assembling GTPases whose common function is to regulate membrane dynamics in a variety of cellular processes. Dnm1, which is a yeast DRP (Drp1/Dlp1 in humans), is required for mitochondrial division, but its mechanism is unknown. We provide evidence that Dnm1 likely functions through self-assembly to drive the membrane constriction event that is associated with...

Read the complete abstract on PubMed

Topics

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

Share to Dimerization
Share to GTP Phosphohydrolases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondria

Share to Mitochondrial Proteins

Share to Mutation

Share to Osmolar Concentration

Share to Protein Conformation

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 16186251
DOI: 10.1083/jcb.200506078
PMCID: PMC2171542

Provenance

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dnm1 forms spirals that are structurally tailored to fit mitochondria.PMID 16186251Read ↗

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

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

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

An intermembrane space protein facilitates completion of mitochondrial division in yeastSemantic proximity Read ↗

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

Mimicking human Drp1 disease-causing mutations in yeast Dnm1 reveals altered mitochondrial dynamics.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 ↗

Disease-associated mutations in Drp1 have fundamentally different effects on the mitochondrial fission machinery.Semantic proximity Read ↗

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

Nanoscale dynamics of Dynamin 1 helices reveals squeeze-twist deformation mode critical for membrane fission.Semantic proximity Read ↗

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