Evidence map›Paper›PMID 37089068›Full record

ReviewTraffic (Copenhagen, Denmark)2023

Out of the ESCPE room: Emerging roles of endosomal SNX-BARs in receptor transport and host-pathogen interaction.

Boris Simonetti, James L Daly, Peter J Cullen

Abstract readReview
In one paragraph

Review in Traffic (Copenhagen, Denmark), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Article
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  5. Sorting nexin 5 mediates antigen presentation and immunity againstbioRxiv : the preprint server for biology · 2026
    Article
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  7. Review
  8. Review
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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

3 authors.

Boris SimonettiCharles River Laboratories, Discovery House, Quays Office Park, Conference Avenue, Portishead, Bristol, UK.ORCID 0000-0002-0304-6640
James L DalyDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, Guy's Hospital, King's College London, London, UK.ORCID 0000-0002-4551-1256
Peter J CullenSchool of Biochemistry, Faculty of Life Sciences, Biomedical Sciences Building, University of Bristol, Bristol, UK.ORCID 0000-0002-9070-8349

Funding

Medical Research Council MR/L007363/1Medical Research Council MR/P018807/1Wellcome TrustWellcome Trust 104568/Z/14/ZWellcome Trust 220260/Z/20/ZWellcome Trust 225128/Z/22/Z
6 · The paper itself

Abstract

Several functions of the human cell, such as sensing nutrients, cell movement and interaction with the surrounding environment, depend on a myriad of transmembrane proteins and their associated proteins and lipids (collectively termed "cargoes"). To successfully perform their tasks, cargo must be sorted and delivered to the right place, at the right time, and in the right amount. To achieve this, eukaryotic cells have evolved a highly organized sorting platform, the endosomal network. Here, a variety of specialized multiprotein complexes sort cargo into itineraries leading to either their degradation or their recycling to various organelles for further rounds of reuse. A key sorting complex is the Endosomal SNX-BAR Sorting Complex for Promoting Exit (ESCPE-1) that promotes the recycling of an array of cargos to the plasma membrane and/or the trans-Golgi network. ESCPE-1 recognizes a hydrophobic-based sorting motif in numerous cargoes and orchestrates their packaging into tubular carriers that pinch off from the endosome and travel to the target organelle. A wide range of pathogens mimic this sorting motif to hijack ESCPE-1 transport to promote their invasion and survival within infected cells. In other instances, ESCPE-1 exerts restrictive functions against pathogens by limiting their replication and infection. In this review, we discuss ESCPE-1 assembly and functions, with a particular focus on recent advances in the understanding of its role in membrane trafficking, cellular homeostasis and host-pathogen interaction.

Indexed as

EndosomesHost-Pathogen InteractionsMultiprotein ComplexesReceptors, Cell SurfaceSorting NexinsChlamydia trachomatisHumansProtein TransportSalmonella typhimuriumtrans-Golgi NetworkVirusesMultiprotein ComplexesReceptors, Cell SurfaceSorting Nexinscell biologyendosomeshost-pathogen interactionsinfectionlysosomesmembranesxenophagy

Identifiers

PMID37089068
PMCPMC10768393

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.