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

A novel role of Mgm1p, a dynamin-related GTPase, in ATP synthase assembly and cristae formation/maintenance.

The Biochemical journal - 1 Jul 2004

Amutha Boominathan, Gordon Donna M, Gu Yajuan, Pain Debkumar

Abstract excerpt

In Saccharomyces cerevisiae, two mitochondrial inner-membrane proteins play critical roles in organellar morphology. One is a dynamin-related GTPase, Mgm1p, which participates in mitochondrial fusion. Another is Tim11p, which is required for oligomeric assembly of F1Fo-ATP synthase, which generates ATP through oxidative phosphorylation. Our data bring these findings together and define a novel role for Mgm1p in...

Read the complete abstract on PubMed

Topics

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

Share to Cytochromes c
Share to GTP-Binding Proteins
Share to Microscopy, Electron

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mitochondrial Proteins

Share to Mitochondrial Proton-Translocating ATPases

Share to Organelles

Share to Proton-Translocating ATPases

Share to Serine Endopeptidases

Source

Open in PubMed Open full text

Identifiers

PMID: 15125685
DOI: 10.1042/BJ20040566
PMCID: PMC1133757

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

A novel role of Mgm1p, a dynamin-related GTPase, in ATP synthase assembly and cristae formation/maintenance.PMID 15125685Read ↗

Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1.Semantic proximity Read ↗

A DRP-like pseudoenzyme coordinates with MICOS to promote cristae architectureSemantic proximity Read ↗

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

[Mitochondrial morphology and dynamics: actors, mechanisms and functions].Semantic proximity Read ↗

Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1.Semantic proximity Read ↗

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

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

Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion.Semantic proximity Read ↗

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

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

Human CCDC51 and yeast Mdm33 are functionally conserved mitochondrial inner membrane proteins that demarcate a subset of organelle fission eventsSemantic proximity Read ↗

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