Evidence map›Paper›PMID 36920342›Full record

ArticleThe Journal of cell biology2023

The exocyst complex is an essential component of the mammalian constitutive secretory pathway.

Conceição Pereira, Danièle Stalder, Georgina S F Anderson, Amber S Shun-Shion, Jack Houghton, Robin Antrobus, Michael A Chapman, Daniel J Fazakerley, David C Gershlick

Open access · hybridFull text read
In one paragraph

Article in The Journal of cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

35 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
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  13. Preassembly and independent trafficking of the exocyst complex inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. The autophagy-specific exocyst subcomplex contributes to phagophore assembly site integrity by promoting phagophore expansion.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  20. Roles for the canonical polarity machinery in thebioRxiv : the preprint server for biology · 2025
    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 1 institution in 1 country.

Conceição Pereira *Cambridge Institute for Medical Research, University of Cambridge , Cambridge, UK.ORCID 0000-0003-0164-4169
Danièle Stalder *Cambridge Institute for Medical Research, University of Cambridge , Cambridge, UK.ORCID 0000-0002-6996-4006
Georgina S F AndersonMRC Toxicology Unit, University of Cambridge , Cambridge, UK.ORCID 0000-0003-4747-1689
Amber S Shun-ShionMetabolic Research Laboratory, Wellcome-Medical Research Council Institute of Metabolic Science, University of Cambridge , Cambridge, UK.ORCID 0000-0001-6439-7893
Jack HoughtonCambridge Institute for Medical Research, University of Cambridge , Cambridge, UK.ORCID 0000-0002-2971-0271
Robin AntrobusCambridge Institute for Medical Research, University of Cambridge , Cambridge, UK.ORCID 0000-0001-8608-4011
Michael A ChapmanMRC Toxicology Unit, University of Cambridge , Cambridge, UK.ORCID 0000-0001-8342-0606
Daniel J FazakerleyMetabolic Research Laboratory, Wellcome-Medical Research Council Institute of Metabolic Science, University of Cambridge , Cambridge, UK.ORCID 0000-0001-8241-2903
David C GershlickCambridge Institute for Medical Research, University of Cambridge , Cambridge, UK.ORCID 0000-0002-0602-210X
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/W005905/1Cancer Research UK 24724Medical Research Council MC_UU_00025/10Medical Research Council MR/S007091/1Wellcome Trust 210481Wellcome Trust 210481/Z/18/Z
6 · The paper itself

Abstract

Secreted proteins fulfill a vast array of functions, including immunity, signaling, and extracellular matrix remodeling. In the trans-Golgi network, proteins destined for constitutive secretion are sorted into post-Golgi carriers which fuse with the plasma membrane. The molecular machinery involved is poorly understood. Here, we have used kinetic trafficking assays and transient CRISPR-KO to study biosynthetic sorting from the Golgi to the plasma membrane. Depletion of all canonical exocyst subunits causes cargo accumulation in post-Golgi carriers. Exocyst subunits are recruited to and co-localize with carriers. Exocyst abrogation followed by kinetic trafficking assays of soluble cargoes results in intracellular cargo accumulation. Unbiased secretomics reveals impairment of soluble protein secretion after exocyst subunit knockout. Importantly, in specialized cell types, the loss of exocyst prevents constitutive secretion of antibodies in lymphocytes and of leptin in adipocytes. These data identify exocyst as the functional tether of secretory post-Golgi carriers at the plasma membrane and an essential component of the mammalian constitutive secretory pathway.

Indexed as

ExocytosisSecretory PathwayAnimalsCell MembraneGolgi ApparatusMammalsProteinsProtein Transporttrans-Golgi NetworkProteins

Identifiers

PMID36920342
PMCPMC10041652
OpenAlexW4324303404

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read79
identifiers read12
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.