Evidence map›Paper›PMID 30640902›Full record

ArticlePloS one2019

Rab32 interacts with SNX6 and affects retromer-dependent Golgi trafficking.

Dieter Waschbüsch, Nicole Hübel, Edith Ossendorf, Evy Lobbestael, Veerle Baekelandt, Andrew J Lindsay, Mary W McCaffrey, Amir R Khan, Angelika Barnekow

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Rab32 regulates Golgi structure and cell migration through Protein Kinase A-mediated phosphorylation of Optineurin.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

9 authors at 4 institutions in 3 countries.

Dieter WaschbüschDepartment of Experimental Tumorbiology, Westfalische Wilhelms University Muenster, Muenster, Germany.
Nicole HübelDepartment of Experimental Tumorbiology, Westfalische Wilhelms University Muenster, Muenster, Germany.
Edith OssendorfDepartment of Experimental Tumorbiology, Westfalische Wilhelms University Muenster, Muenster, Germany.
Evy LobbestaelLaboratory for Neurobiology and Gene Therapy, KU Leuven, Leuven, Belgium.
Veerle BaekelandtLaboratory for Neurobiology and Gene Therapy, KU Leuven, Leuven, Belgium.
Andrew J LindsaySchool of Biochemistry and Cell Biology, Biosciences Institute, University College Cork, Cork, Ireland.
Mary W McCaffreySchool of Biochemistry and Cell Biology, Biosciences Institute, University College Cork, Cork, Ireland.
Amir R KhanSchool of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland.ORCID 0000-0003-1176-6952
Angelika BarnekowDepartment of Experimental Tumorbiology, Westfalische Wilhelms University Muenster, Muenster, Germany.
University of Münster · DEKU Leuven · BETrinity College Dublin · IEUniversity College Cork · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Rab family of small GTPases regulate various aspects of cellular dynamics in eukaryotic cells. Membrane trafficking has emerged as central to the functions of leucine-rich repeat kinase 2 (LRRK2), which is associated with inherited and sporadic forms of Parkinson's disease (PD). Rabs act as both regulators of the catalytic activity and targets for serine/threonine phosphorylation by LRRK2. Rab32, Rab38 and Rab29 have been shown to regulate LRRK2 sub-cellular localization through direct interactions. Recently, Rab29 was shown to escort LRRK2 to the Golgi apparatus and activate the phosphorylation of Rab8 and Rab10. Rab32 is linked to multiple cellular functions including endosomal trafficking, mitochondrial dynamics, and melanosome biogenesis. A missense mutation in Rab32 has also recently been linked to PD. Here, we demonstrate that Rab32 directly interacts with sorting nexin 6 (SNX6). SNX6 is a transient subunit of the retromer, an endosome-Golgi retrieval complex whose Vps35 subunit is strongly associated with PD. We could further show that localization of cation-independent mannose-6-phosphate receptors, which are recycled to the trans-Golgi network (TGN) by the retromer, was affected by both Rab32 and SNX6. These data imply that Rab32 is linked to SNX6/retromer trafficking at the Golgi, and also suggests a possible connection between the retromer and Rab32 in the trafficking and biological functions of LRRK2.

Indexed as

Blotting, WesternCell LineFluorescent Antibody TechniqueGolgi ApparatusHumansImmunoprecipitationProtein Bindingrab GTP-Binding ProteinsSorting Nexinstrans-Golgi NetworkTwo-Hybrid System TechniquesRab32 protein, humanRAB38 protein, humanrab GTP-Binding ProteinsSNX6 protein, humanSorting Nexins

Identifiers

PMID30640902
PMCPMC6331118
OpenAlexW2909661883

What OpenQuestion holds

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LicenceCC BY
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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.