Evidence map›Paper›PMID 27354379›Full record

ArticleThe Journal of cell biology2016

Phosphatidylserine transport by Ups2-Mdm35 in respiration-active mitochondria.

Non Miyata, Yasunori Watanabe, Yasushi Tamura, Toshiya Endo, Osamu Kuge

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

46 citing papers in PubMed, 80 citations in OpenAlex.

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  10. microPublication biology · 2023
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  19. Quality control of the mitochondrial proteome.Nature reviews. Molecular cell biology · 2021
    Review
  20. Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020
    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

5 authors at 3 institutions in 1 country.

Non MiyataDepartment of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan.ORCID 0000-0002-5945-909X
Yasunori WatanabeFaculty of Life Sciences, Kyoto Sangyo University, Kyoto 603-8555, Japan.
Yasushi TamuraDepartment of Material and Biological Chemistry, Faculty of Science, Yamagata University, Yamagata 990-8560, Japan.ORCID 0000-0002-8462-0607
Toshiya EndoFaculty of Life Sciences, Kyoto Sangyo University, Kyoto 603-8555, Japan.
Osamu KugeDepartment of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan kuge@chem.kyushu-univ.jp.ORCID 0000-0003-4962-3519
Kyoto Sangyo University · JPKyushu University · JPYamagata University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphatidylethanolamine (PE) is an essential phospholipid for mitochondrial functions and is synthesized mainly by phosphatidylserine (PS) decarboxylase at the mitochondrial inner membrane. In Saccharomyces cerevisiae, PS is synthesized in the endoplasmic reticulum (ER), such that mitochondrial PE synthesis requires PS transport from the ER to the mitochondrial inner membrane. Here, we provide evidence that Ups2-Mdm35, a protein complex localized at the mitochondrial intermembrane space, mediates PS transport for PE synthesis in respiration-active mitochondria. UPS2- and MDM35-null mutations greatly attenuated conversion of PS to PE in yeast cells growing logarithmically under nonfermentable conditions, but not fermentable conditions. A recombinant Ups2-Mdm35 fusion protein exhibited phospholipid-transfer activity between liposomes in vitro. Furthermore, UPS2 expression was elevated under nonfermentable conditions and at the diauxic shift, the metabolic transition from glycolysis to oxidative phosphorylation. These results demonstrate that Ups2-Mdm35 functions as a PS transfer protein and enhances mitochondrial PE synthesis in response to the cellular metabolic state.

Indexed as

Biological TransportCell RespirationFermentationGene DeletionMitochondriaMitochondrial ProteinsMutationPhosphatidylethanolaminesPhosphatidylserinesPhospholipid Transfer ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMdm35 protein, S cerevisiaeMitochondrial ProteinsphosphatidylethanolaminePhosphatidylethanolaminesPhosphatidylserinesPhospholipid Transfer ProteinsSaccharomyces cerevisiae ProteinsUps2 protein, S cerevisiae

Identifiers

PMID27354379
PMCPMC4932372
OpenAlexW2460215877

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.