Evidence map›Paper›PMID 25117470›Full record

ArticlePloS one2014

Proteomic analysis reveals a novel function of the kinase Sat4p in Saccharomyces cerevisiae mitochondria.

Uta Gey, Cornelia Czupalla, Bernard Hoflack, Udo Krause, Gerhard Rödel

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Mechanism-Driven Metabolic Engineering for Bio-Based Production of FreeFrontiers in bioengineering and biotechnology · 2020
    Article
  6. Article
  7. Article
  8. Functional Analysis of the FZF1 Genes ofFrontiers in microbiology · 2018
    Article
  9. Article
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 1 institution in 1 country.

Uta GeyInstitute of Genetics, Technische Universität Dresden, Dresden, Germany.
Cornelia CzupallaBiotechnological Center, Technische Universität Dresden, Dresden, Germany.
Bernard HoflackBiotechnological Center, Technische Universität Dresden, Dresden, Germany.
Udo KrauseInstitute of Genetics, Technische Universität Dresden, Dresden, Germany.
Gerhard RödelInstitute of Genetics, Technische Universität Dresden, Dresden, Germany.
TU Dresden · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Saccharomyces cerevisiae kinase Sat4p has been originally identified as a protein involved in salt tolerance and stabilization of plasma membrane transporters, implicating a cytoplasmic localization. Our study revealed an additional mitochondrial (mt) localization, suggesting a dual function for Sat4p. While no mt related phenotype was observed in the absence of Sat4p, its overexpression resulted in significant changes of a specific mitochondrial subproteome. As shown by a comparative two dimensional difference gel electrophoresis (2D-DIGE) approach combined with mass spectrometry, particularly two groups of proteins were affected: the iron-sulfur containing aconitase-type proteins (Aco1p, Lys4p) and the lipoamide-containing subproteome (Lat1p, Kgd2p and Gcv3p). The lipoylation sites of all three proteins could be assigned by nanoLC-MS/MS to Lys75 (Lat1p), Lys114 (Kgd2p) and Lys102 (Gcv3p), respectively. Sat4p overexpression resulted in accumulation of the delipoylated protein variants and in reduced levels of aconitase-type proteins, accompanied by a decrease in the activities of the respective enzyme complexes. We propose a regulatory role of Sat4p in the late steps of the maturation of a specific subset of mitochondrial iron-sulfur cluster proteins, including Aco1p and lipoate synthase Lip5p. Impairment of the latter enzyme may account for the observed lipoylation defects.

Indexed as

ProteomicsCytoplasmGene ExpressionIntracellular Signaling Peptides and ProteinsMitochondriaMitochondrial ProteinsModels, BiologicalMultiprotein ComplexesProtein Serine-Threonine KinasesProtein TransportProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsIntracellular Signaling Peptides and ProteinsMitochondrial ProteinsMultiprotein ComplexesProtein Serine-Threonine KinasesProteomeSaccharomyces cerevisiae ProteinsSAT4 protein, S cerevisiae

Identifiers

PMID25117470
PMCPMC4138037
OpenAlexW2017703237

What OpenQuestion holds

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LicenceCC BY
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.