Evidence map›Paper›PMID 22403410›Full record

ArticleThe Journal of biological chemistry2012

Role for two conserved intermembrane space proteins, Ups1p and Ups2p, [corrected] in intra-mitochondrial phospholipid trafficking.

Yasushi Tamura, Ouma Onguka, Alyson E Aiken Hobbs, Robert E Jensen, Miho Iijima, Steven M Claypool, Hiromi Sesaki

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 67 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 1 pooled it
5.0field-weighted citation impact, top 4% 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

67 citing papers in PubMed, 1 synthesis or guideline pooled it, 108 citations in OpenAlex.

  1. Pooled it
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  11. Human Sterols Are Overproduced, Stored and Excreted in Yeasts.International journal of molecular sciences · 2024
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7 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Yasushi TamuraDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. ytamura1@jhmi.edu
Ouma Onguka
Alyson E Aiken Hobbs
Robert E Jensen
Miho Iijima
Steven M Claypool
Hiromi Sesaki
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
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 GM084015NIGMS NIH HHS GM089853NIGMS NIH HHS R01 GM084015NIGMS NIH HHS R01 GM089853NIGMS NIH HHS T32 GM007445
6 · The paper itself

Abstract

Mitochondrial membranes maintain a specific phospholipid composition. Most phospholipids are synthesized in the endoplasmic reticulum (ER) and transported to mitochondria, but cardiolipin and phosphatidylethanolamine are produced in mitochondria. In the yeast Saccharomyces cerevisiae, phospholipid exchange between the ER and mitochondria relies on the ER-mitochondria encounter structure (ERMES) complex, which physically connects the ER and mitochondrial outer membrane. However, the proteins and mechanisms involved in phospholipid transport within mitochondria remain elusive. Here, we investigated the role of the conserved intermembrane space proteins, Ups1p and Ups2p, and an inner membrane protein, Mdm31p, in phospholipid metabolism. Our data show that loss of the ERMES complex, Ups1p, and Mdm31p causes similar defects in mitochondrial phospholipid metabolism, mitochondrial morphology, and cell growth. Defects in cells lacking the ERMES complex or Ups1p are suppressed by Mdm31p overexpression as well as additional loss of Ups2p, which antagonizes Ups1p. Combined loss of the ERMES complex and Ups1p exacerbates phospholipid defects. Finally, pulse-chase experiments using [(14)C]serine revealed that Ups1p and Ups2p antagonistically regulate conversion of phosphatidylethanolamine to phosphatidylcholine. Our results suggest that Ups proteins and Mdm31p play important roles in phospholipid biosynthesis in mitochondria. Ups proteins may function in phospholipid trafficking between the outer and inner mitochondrial membranes.

Indexed as

Biological TransportBlotting, WesternEndoplasmic ReticulumHydrogen-Ion ConcentrationIntracellular MembranesMembrane ProteinsMicroscopy, FluorescenceMitochondrial MembranesMitochondrial ProteinsMutationPhosphatidylethanolaminesPhosphatidylserinesPhospholipidsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSerineMDM10 protein, S cerevisiaeMdm31 protein, S cerevisiaeMembrane ProteinsMitochondrial ProteinsMMM1 protein, S cerevisiaeMMM2 protein, S cerevisiaephosphatidylethanolaminePhosphatidylethanolaminesPhosphatidylserinesPhospholipidsSaccharomyces cerevisiae ProteinsSerineUps1 protein, S cerevisiaeUps2 protein, S cerevisiae

Identifiers

PMID22403410
PMCPMC3346110
OpenAlexW2048227985

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.