Evidence map›Paper›PMID 30804014›Full record

ArticleEMBO reports2019

Cytoplasmic control of Rab family small GTPases through BAG6.

Toshiki Takahashi, Setsuya Minami, Yugo Tsuchiya, Kazu Tajima, Natsumi Sakai, Kei Suga, Shin-Ichi Hisanaga, Norihiko Ohbayashi, Mitsunori Fukuda, Hiroyuki Kawahara

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

25 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  5. VPS29C: Adding complexity to the Retromer complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  8. Review
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  15. Phosphorylation of Arl4A/D promotes their binding by the HYPK chaperone for their stable recruitment to the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
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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

10 authors at 4 institutions in 1 country.

Toshiki TakahashiLaboratory of Cell Biology and Biochemistry, Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, Japan.
Setsuya MinamiLaboratory of Cell Biology and Biochemistry, Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, Japan.
Yugo TsuchiyaLaboratory of Cell Biology and Biochemistry, Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, Japan.
Kazu TajimaLaboratory of Cell Biology and Biochemistry, Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, Japan.
Natsumi SakaiLaboratory of Cell Biology and Biochemistry, Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, Japan.
Kei SugaDepartment of Cell Physiology, Kyorin University School of Medicine, Mitaka, Japan.
Shin-Ichi HisanagaLaboratory of Molecular Neuroscience, Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, Japan.
Norihiko OhbayashiDepartment of Physiological Chemistry, Faculty of Medicine, University of Tsukuba, Tsukuba, Japan.
Mitsunori FukudaDepartment of Integrative Life Sciences, Graduate School of Life Sciences, Tohoku University, Sendai, Japan.ORCID 0000-0002-8620-5853
Hiroyuki KawaharaLaboratory of Cell Biology and Biochemistry, Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, Japan hkawa@tmu.ac.jp.ORCID 0000-0001-8506-9012
Tokyo Metropolitan University · JPKyorin University · JPTohoku University · JPUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rab family small GTPases are master regulators of distinct steps of intracellular vesicle trafficking in eukaryotic cells. GDP-bound cytoplasmic forms of Rab proteins are prone to aggregation due to the exposure of hydrophobic groups but the machinery that determines the fate of Rab species in the cytosol has not been elucidated in detail. In this study, we find that BAG6 (BAT3/Scythe) predominantly recognizes a cryptic portion of GDP-associated Rab8a, while its major GTP-bound active form is not recognized. The hydrophobic residues of the Switch I region of Rab8a are essential for its interaction with BAG6 and the degradation of GDP-Rab8a via the ubiquitin-proteasome system. BAG6 prevents the excess accumulation of inactive Rab8a, whose accumulation impairs intracellular membrane trafficking. BAG6 binds not only Rab8a but also a functionally distinct set of Rab family proteins, and is also required for the correct distribution of Golgi and endosomal markers. From these observations, we suggest that Rab proteins represent a novel set of substrates for BAG6, and the BAG6-mediated pathway is associated with the regulation of membrane vesicle trafficking events in mammalian cells.

Indexed as

Amino Acid SequenceAnimalsCell LineCell MembraneCytoplasmCytosolEndoplasmic ReticulumEndosomesGene DeletionGolgi ApparatusHumansModels, BiologicalMolecular ChaperonesProtein BindingProtein Interaction Domains and MotifsProtein TransportBAG6 protein, humanMolecular ChaperonesRAB8A protein, humanrab GTP-Binding ProteinsRNA, Small InterferingUbiquitinBAG6membrane traffickingRab8aRab GTP‐binding proteinsubiquitin‐proteasome system

Identifiers

PMID30804014
PMCPMC6446207
OpenAlexW2917780097

What OpenQuestion holds

Textmetadata
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.