Evidence map›Paper›PMID 39514288›Full record

ArticleThe Journal of cell biology2024

BEACH domain proteins function as cargo-sorting adaptors in secretory and endocytic pathways.

Serhiy Pankiv, Anette Kathinka Dahl, Aleksander Aas, Rosa Linn Andersen, Andreas Brech, Petter Holland, Sakshi Singh, Christian Bindesbøll, Anne Simonsen

Abstract read
In one paragraph

Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. WDFY4-dependent cross-presentation proceeds via a vacuolar antigen-processing route.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Proteostasis of immune checkpoint receptors.The Biochemical journal · 2025
    Review
  4. ThemSphere · 2025
    Article
  5. Article
  6. The winding road to platelet α-granules.Frontiers in cell and developmental biology · 2025
    Review
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.

Serhiy PankivDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.ORCID 0000-0001-7953-2445
Anette Kathinka DahlDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.ORCID 0000-0001-7278-0454
Aleksander AasDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.ORCID 0009-0005-1721-494X
Rosa Linn AndersenCentre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo , Oslo, Norway.ORCID 0009-0001-6544-963X
Andreas BrechCentre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo , Oslo, Norway.ORCID 0000-0002-9803-1774
Petter HollandDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.ORCID 0000-0002-5717-6985
Sakshi SinghDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.ORCID 0000-0002-2168-1066
Christian BindesbøllDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.ORCID 0009-0002-2326-4415
Anne SimonsenDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.ORCID 0000-0003-4711-7057

Funding

Marie Skłodowska-CurieNorwegian Cancer Society 190251Research Council of Norway 262652South-Eastern Norway Regional Health Authority
6 · The paper itself

Abstract

We identify BEACH domain-containing proteins (BDCPs) as novel membrane coat proteins involved in the sorting of transmembrane proteins (TMPs) on the trans-Golgi network and tubular sorting endosomes. The seven typical mammalian BDCPs share a predicted alpha-solenoid-beta propeller structure, suggesting they have a protocoatomer origin and function. We map the subcellular localization of seven BDCPs based on their dynamic colocalization with RAB and ARF small GTPases and identify five typical BDCPs on subdomains of dynamic tubular-vesicular compartments on the intersection of endocytic recycling and post-Golgi secretory pathways. We demonstrate that BDCPs interact directly with the cytosolic tails of selected TMPs and identify a subset of TMPs, whose trafficking to the plasma membrane is affected in cells lacking BDCP. We propose that the competitive binding of BDCPs and clathrin coat adaptors to the cytosolic tails of TMPs, followed by their clustering to distinct subdomains of secretory/recycling tubules function as a mechanism for sorting of TMPs in pleomorphic tubular-vesicular compartments that lack a clathrin coat.

Indexed as

EndocytosisEndosomesProtein Transporttrans-Golgi NetworkAdaptor Proteins, Vesicular TransportADP-Ribosylation FactorsAnimalsCell MembraneHeLa CellsHumansMembrane ProteinsProtein BindingProtein Domainsrab GTP-Binding ProteinsSecretory PathwayAdaptor Proteins, Vesicular TransportADP-Ribosylation FactorsMembrane Proteinsrab GTP-Binding Proteins

Identifiers

PMID39514288
PMCPMC11554844

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.