Evidence map›Paper›PMID 35019937›Full record

ArticleThe Journal of cell biology2022

Regulating peroxisome-ER contacts via the ACBD5-VAPB tether by FFAT motif phosphorylation and GSK3β.

Suzan Kors, Christian Hacker, Chloe Bolton, Renate Maier, Lena Reimann, Emily J A Kitchener, Bettina Warscheid, Joseph L Costello, Michael Schrader

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

41 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Peroxisome calcium uptake is dependent on ER-peroxisome membrane contact.Cellular and molecular life sciences : CMLS · 2026
    Article
  6. Article
  7. Article
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  9. Review
  10. Article
  11. Article
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  14. Article
  15. Review
  16. Article
  17. Imaging interorganelle contacts at a glance.Journal of cell science · 2024
    Review
  18. Article
  19. Article
  20. 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

9 authors at 2 institutions in 2 countries.

Suzan KorsCollege of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter, UK.ORCID 0000-0002-8135-143X
Christian HackerCollege of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter, UK.
Chloe BoltonCollege of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter, UK.ORCID 0000-0001-5422-725X
Renate MaierInstitute of Biology II, Biochemistry and Functional Proteomics, Faculty of Biology, University of Freiburg, Freiburg, Germany.
Lena ReimannInstitute of Biology II, Biochemistry and Functional Proteomics, Faculty of Biology, University of Freiburg, Freiburg, Germany.ORCID 0000-0001-5465-5895
Emily J A KitchenerCollege of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter, UK.
Bettina WarscheidInstitute of Biology II, Biochemistry and Functional Proteomics, Faculty of Biology, University of Freiburg, Freiburg, Germany.ORCID 0000-0001-5096-1975
Joseph L Costello *College of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter, UK.ORCID 0000-0002-2867-1864
Michael Schrader *College of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter, UK.ORCID 0000-0003-2146-0535
University of Exeter · GBUniversity of Freiburg · DE

Funding

Biotechnology and Biological Sciences Research Council BB/N01541X/1Marie Curie 812968 PERICOMedical Research Council CiC 08135Medical Research Council MR/N0137941/1Medical Research Council MR/T019409/1
6 · The paper itself

Abstract

Peroxisomes and the endoplasmic reticulum (ER) cooperate in cellular lipid metabolism. They form membrane contacts through interaction of the peroxisomal membrane protein ACBD5 (acyl-coenzyme A-binding domain protein 5) and the ER-resident protein VAPB (vesicle-associated membrane protein-associated protein B). ACBD5 binds to the major sperm protein domain of VAPB via its FFAT-like (two phenylalanines [FF] in an acidic tract) motif. However, molecular mechanisms, which regulate formation of these membrane contact sites, are unknown. Here, we reveal that peroxisome-ER associations via the ACBD5-VAPB tether are regulated by phosphorylation. We show that ACBD5-VAPB binding is phosphatase-sensitive and identify phosphorylation sites in the flanking regions and core of the FFAT-like motif, which alter interaction with VAPB-and thus peroxisome-ER contact sites-differently. Moreover, we demonstrate that GSK3β (glycogen synthase kinase-3 β) regulates this interaction. Our findings reveal for the first time a molecular mechanism for the regulation of peroxisome-ER contacts in mammalian cells and expand the current model of FFAT motifs and VAP interaction.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsCell LineEndoplasmic ReticulumGlycogen Synthase Kinase 3 betaHumansMembrane ProteinsMiceMutationPeroxisomesPhosphorylationPhosphoserineProtein BindingVesicular Transport ProteinsACBD5 protein, humanAdaptor Proteins, Signal TransducingGlycogen Synthase Kinase 3 betaMembrane ProteinsPhosphoserineVAPB protein, humanVesicular Transport Proteins

Identifiers

PMID35019937
PMCPMC8759595
OpenAlexW4220916290

What Socratic 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 Socratic graph.