Evidence map›Paper›PMID 26627908›Full record

ArticleScientific reports2015

Conserved targeting information in mammalian and fungal peroxisomal tail-anchored proteins.

Judith Buentzel, Fabio Vilardi, Amelie Lotz-Havla, Jutta Gärtner, Sven Thoms

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

8 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural Mapping of Missense Mutations in the Pex1/Pex6 Complex.International journal of molecular sciences · 2019
    Review
  4. Review
  5. Article
  6. The peroxisome: an update on mysteries 2.0.Histochemistry and cell biology · 2018
    Review
  7. Review
  8. 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.

Judith BuentzelUniversity Medical Center, Department of Child and Adolescent Medicine, Robert Koch Str. 40, 37075 Göttingen, Germany.
Fabio VilardiDepartment of Molecular Biology, Humboldtallee 23, 37073 Göttingen, Germany.
Amelie Lotz-HavlaDr. von Haunersches Kinderspital, Lindwurmstr. 2a, 80337 München.
Jutta GärtnerUniversity Medical Center, Department of Child and Adolescent Medicine, Robert Koch Str. 40, 37075 Göttingen, Germany.
Sven ThomsUniversity Medical Center, Department of Child and Adolescent Medicine, Robert Koch Str. 40, 37075 Göttingen, Germany.
University of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The targeting signals and mechanisms of soluble peroxisomal proteins are well understood, whereas less is known about the signals and targeting routes of peroxisomal membrane proteins (PMP). Pex15 and PEX26, tail-anchored proteins in yeast and mammals, respectively, exert a similar cellular function in the recruitment of AAA peroxins at the peroxisomal membrane. But despite their common role, Pex15 and PEX26 are neither homologs nor they are known to follow similar targeting principles. Here we show that Pex15 targets to peroxisomes in mammalian cells, and PEX26 reaches peroxisomes when expressed in yeast cells. In both proteins C-terminal targeting information is sufficient for correct sorting to the peroxisomal membrane. In yeast, PEX26 follows the pathway that also ensures correct targeting of Pex15: PEX26 enters the endoplasmic reticulum (ER) in a GET-dependent and Pex19-independent manner. Like in yeast, PEX26 enters the ER in mammalian cells, however, independently of GET/TRC40. These data show that conserved targeting information is employed in yeast and higher eukaryotes during the biogenesis of peroxisomal tail-anchored proteins.

Indexed as

Arsenite Transporting ATPasesHeLa CellsHumansMembrane ProteinsPeroxisomesPhosphoproteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsArsenite Transporting ATPasesGET3 protein, humanMembrane ProteinsPEX15 protein, S cerevisiaePEX26 protein, humanPhosphoproteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID26627908
PMCPMC4667187
OpenAlexW2192140425

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.