Evidence map›Paper›PMID 28542518›Full record

ArticlePloS one2017

RNF41 interacts with the VPS52 subunit of the GARP and EARP complexes.

Delphine Masschaele, Leentje De Ceuninck, Joris Wauman, Dieter Defever, Frank Stenner, Sam Lievens, Frank Peelman, Jan Tavernier

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. GARP Complex in Golgi Physiology.Sub-cellular biochemistry · 2026
    Review
  3. Article
  4. Article
  5. Role of GARP Vesicle Tethering Complex in Golgi Physiology.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. GZFLW Induces Apoptosis of Ectopic Endometrial Stromal Cells via Promoting VPS53 Protein Stability.Evidence-based complementary and alternative medicine : eCAM · 2018
    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

8 authors at 3 institutions in 2 countries.

Delphine MasschaeleCytokine Receptor Laboratory, Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium.
Leentje De CeuninckCytokine Receptor Laboratory, Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium.
Joris WaumanCytokine Receptor Laboratory, Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium.
Dieter DefeverCytokine Receptor Laboratory, Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium.
Frank StennerDepartment of Oncology, University Hospital Basel, University of Basel, Basel, Switzerland.
Sam LievensCytokine Receptor Laboratory, Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium.
Frank PeelmanCytokine Receptor Laboratory, Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium.
Jan TavernierCytokine Receptor Laboratory, Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium.
VIB-UGent Center for Medical Biotechnology · BEGhent University · BEUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNF41 (Ring Finger Protein 41) is an E3 ubiquitin ligase involved in the intracellular sorting and function of a diverse set of substrates. Next to BRUCE and Parkin, RNF41 can directly ubiquitinate ErbB3, IL-3, EPO and RARα receptors or downstream signaling molecules such as Myd88, TBK1 and USP8. In this way it can regulate receptor signaling and routing. To further elucidate the molecular mechanism behind the role of RNF41 in intracellular transport we performed an Array MAPPIT (Mammalian Protein-Protein Interaction Trap) screen using an extensive set of proteins derived from the human ORFeome collection. This paper describes the identification of VPS52, a subunit of the GARP (Golgi-Associated Retrograde Protein) and the EARP (Endosome-Associated Recycling Protein) complexes, as a novel interaction partner of RNF41. Through interaction via their coiled coil domains, RNF41 ubiquitinates and relocates VPS52 away from VPS53, a common subunit of the GARP and EARP complexes, towards RNF41 bodies.

Indexed as

EndosomesGolgi ApparatusHeLa CellsHumansMembrane ProteinsMultiprotein ComplexesUbiquitin-Protein LigasesVesicular Transport ProteinsLRRC32 protein, humanMembrane ProteinsMultiprotein ComplexesRNF41 protein, humanUbiquitin-Protein LigasesVesicular Transport ProteinsVPS52 protein, human

Identifiers

PMID28542518
PMCPMC5439944
OpenAlexW2617239187

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.