Evidence map›Paper›PMID 37540145›Full record

ArticleThe Journal of cell biology2023

Completion of mitochondrial division requires the intermembrane space protein Mdi1/Atg44.

Olivia M Connor, Srujan K Matta, Jonathan R Friedman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Ecm19 coordinates mitochondrial fission and cellular redox homeostasis.Redox report : communications in free radical research · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Olivia M ConnorDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0001-7339-3210
Srujan K MattaDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0002-6949-7954
Jonathan R FriedmanDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0001-8155-2429
The University of Texas Southwestern Medical Center · US

Funding

UT Southwestern Medical Center Simmons Comprehensive Cancer CenterP30CA142543 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI MELANIE H. COBB · 2010 to 2026
$53.7M
UT Southwestern NORCP30DK127984 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI Jeff G McDonald · 2022 to 2026
$7.4M
Spatial Organization of the Mitochondrial Inner MembraneR35GM137894 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI Jonathan R. Friedman · 2020 to 2026
$3.1M
Spinning Disk Confocal for UT SouthwesternS10OD028630 · OD · UT SOUTHWESTERN MEDICAL CENTER · PI LUBY-PHELPS, KATHERINE J · 2020 to 2020
$600k
NCI NIH HHS P30 CA142543NIDDK NIH HHS P30 DK127984NIGMS NIH HHS R35 GM137894NIH HHS S10 OD028630
6 · The paper itself

Abstract

Mitochondria are highly dynamic double membrane-bound organelles that maintain their shape in part through fission and fusion. Mitochondrial fission is performed by a dynamin-related protein, Dnm1 (Drp1 in humans), that constricts and divides the mitochondria in a GTP hydrolysis-dependent manner. However, it is unclear whether factors inside mitochondria help coordinate the process and if Dnm1/Drp1 activity is sufficient to complete the fission of both mitochondrial membranes. Here, we identify an intermembrane space protein required for mitochondrial fission in yeast, which we propose to name Mdi1 (also named Atg44). Loss of Mdi1 causes mitochondrial hyperfusion due to defects in fission, but not the lack of Dnm1 recruitment to mitochondria. Mdi1 is conserved in fungal species, and its homologs contain an amphipathic α-helix, mutations of which disrupt mitochondrial morphology. One model is that Mdi1 distorts mitochondrial membranes to enable Dnm1 to robustly complete fission. Our work reveals that Dnm1 cannot efficiently divide mitochondria without the coordinated function of Mdi1 inside mitochondria.

Indexed as

Mitochondrial DynamicsMitochondrial ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDynaminsGTP PhosphohydrolasesMitochondriaMitochondrial MembranesDNM1 protein, S cerevisiaeDynaminsGTP PhosphohydrolasesMitochondrial ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID37540145
PMCPMC10403340
OpenAlexW4385564852

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.