Evidence map›Paper›PMID 16754953›Full record

ArticleThe Journal of cell biology2006

Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p.

Hiromi Sesaki, Cory D Dunn, Miho Iijima, Kelly A Shepard, Michael P Yaffe, Carolyn E Machamer, Robert E Jensen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

51 citing papers in PubMed, 101 citations in OpenAlex.

  1. Mitochondrial membrane remodeling in stress adaptation: Lipid control of organelle quality.Protein science : a publication of the Protein Society · 2026
    Review
  2. Article
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  5. Article
  6. Article
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  10. Article
  11. Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020
    Review
  12. Review
  13. Proteolytic Control of Lipid Metabolism.ACS chemical biology · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Hiromi SesakiDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. hsesaki@jhmi.edu
Cory D Dunn
Miho Iijima
Kelly A Shepard
Michael P Yaffe
Carolyn E Machamer
Robert E Jensen
Johns Hopkins University · USJohns Hopkins Medicine · USUniversity of California, San Diego · US

Funding

MECHANISMS OF MITOCHONDRIAL DIVISION AND INHERITANCER01GM044614 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI YAFFE, MICHAEL P. · 1993 to 2004
$1.4M
PROTEIN IMPORT INTO YEAST MITOCHONDRIAR01GM046803 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JENSEN, ROBERT E · 1993 to 2004
$1.4M
NIGMS NIH HHS GM44614NIGMS NIH HHS GM46803NIGMS NIH HHS R01 GM044614NIGMS NIH HHS R01 GM046803
6 · The paper itself

Abstract

Mgm1p is a conserved dynamin-related GTPase required for fusion, morphology, inheritance, and the genome maintenance of mitochondria in Saccharomyces cerevisiae. Mgm1p undergoes unconventional processing to produce two functional isoforms by alternative topogenesis. Alternative topogenesis involves bifurcate sorting in the inner membrane and intramembrane proteolysis by the rhomboid protease Pcp1p. Here, we identify Ups1p, a novel mitochondrial protein required for the unique processing of Mgm1p and for normal mitochondrial shape. Our results demonstrate that Ups1p regulates the sorting of Mgm1p in the inner membrane. Consistent with its function, Ups1p is peripherally associated with the inner membrane in the intermembrane space. Moreover, the human homologue of Ups1p, PRELI, can fully replace Ups1p in yeast cells. Together, our findings provide a conserved mechanism for the alternative topogenesis of Mgm1p and control of mitochondrial morphology.

Indexed as

GTP-Binding ProteinsHumansMitochondriaMitochondrial MembranesMitochondrial ProteinsProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGTP-Binding ProteinsMGM1 protein, S cerevisiaeMitochondrial ProteinsPRELID1 protein, humanProteinsSaccharomyces cerevisiae ProteinsUps1 protein, S cerevisiae

Identifiers

PMID16754953
PMCPMC2063882
OpenAlexW2046549466

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.