Evidence map›Paper›PMID 20622808›Full record

ArticleThe EMBO journal2010

Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation.

Yasushi Tamura, Miho Iijima, Hiromi Sesaki

Abstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

42 citing papers in PubMed, 74 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
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  11. Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020
    Review
  12. Article
  13. Proteolytic Control of Lipid Metabolism.ACS chemical biology · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. AEMBO reports · 2017
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Yasushi TamuraDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Miho Iijima
Hiromi Sesaki
Johns Hopkins University · US

Funding

Lipid Signaling in ChemotaxisR01GM084015 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI IIJIMA, MIHO · 2009 to 2019
$2.9M
Mitochondrial Fusion and DivisionR01GM089853 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SESAKI, HIROMI · 2010 to 2014
$2.1M
NIGMS NIH HHS R01 GM084015NIGMS NIH HHS R01 GM089853
6 · The paper itself

Abstract

Ups1p, Ups2p, and Ups3p are three homologous proteins that control phospholipid metabolism in the mitochondrial intermembrane space (IMS). The Ups proteins are atypical IMS proteins in that they lack the two major IMS-targeting signals, bipartite presequences and cysteine motifs. Here, we show that Ups protein import is mediated by another IMS protein, Mdm35p. In vitro import assays show that import of Ups proteins requires Mdm35p. Loss of Mdm35p led to a decrease in steady state levels of Ups proteins in mitochondria. In addition, mdm35Delta cells displayed a similar phenotype to ups1Deltaups2Deltaups3Delta cells. Interestingly, unlike typical import machineries, Mdm35p associated stably with Ups proteins at a steady state after import. Demonstrating that Mdm35p is a functional component of Ups-Mdm35p complexes, restoration of Ups protein levels in mdm35Delta mitochondria failed to restore phospholipid metabolism. These findings provide a novel mechanism in which the formation of functional protein complexes drives mitochondrial protein import.

Indexed as

Gene DeletionMicrobial ViabilityMitochondrial MembranesMitochondrial ProteinsModels, BiologicalPhospholipidsProtein BindingProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMdm35 protein, S cerevisiaeMitochondrial ProteinsPhospholipidsSaccharomyces cerevisiae ProteinsUps1 protein, S cerevisiaeUps2 protein, S cerevisiaeUps3 protein, S cerevisiae

Identifiers

PMID20622808
PMCPMC2944057
OpenAlexW2022630511

What OpenQuestion holds

Textmetadata
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.