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

Structural basis of mitochondrial receptor binding and constriction by DRP1.

Nature - 1 Jun 2018

Kalia Raghav, Wang Ray Yu-Ruei, Yusuf Ali, Thomas Paul V, Agard David A, Shaw Janet M, Frost Adam

Abstract excerpt

Mitochondrial inheritance, genome maintenance and metabolic adaptation depend on organelle fission by dynamin-related protein 1 (DRP1) and its mitochondrial receptors. DRP1 receptors include the paralogues mitochondrial dynamics proteins of 49 and 51 kDa (MID49 and MID51) and mitochondrial fission factor (MFF); however, the mechanisms by which these proteins recruit and regulate DRP1 are unknown. Here we present...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Cryoelectron Microscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Death-Associated Protein Kinases

Share to GTP Phosphohydrolases

Share to Guanosine Triphosphate

Share to Hydrolysis

Share to Peptide Elongation Factors

Share to Rotation

Source

Open in PubMed Open full text

Identifiers

PMID: 29899447
DOI: 10.1038/s41586-018-0211-2
PMCID: PMC6120343

Genes

MFF

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

Structural basis of mitochondrial receptor binding and constriction by DRP1.PMID 29899447Read ↗

Structural Basis of Mitochondrial Receptor Binding and GTP-Driven Conformational Constriction by Dynamin-Related Protein 1Semantic proximity Read ↗

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

Opa1 helical structures give perspective to mitochondrial dysfunctionSemantic proximity Read ↗

Impaired turnover of hyperfused mitochondria in severe axonal neuropathy due to a novel DRP1 mutation.Semantic proximity Read ↗

NMR identification of a conserved Drp1 cardiolipin-binding motif essential for stress-induced mitochondrial fission.Semantic proximity Read ↗

Serine 39 in the GTP-binding domain of Drp1 is involved in shaping mitochondrial morphology.Semantic proximity Read ↗

Mitochondrial dynamics and its impact on human health and diseases: inside the DRP1 blackbox.Semantic proximity Read ↗

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

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 ↗

Human Fis1 directly interacts with Drp1 in an evolutionarily conserved manner to promote mitochondrial fissionSemantic proximity Read ↗

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

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