Evidence map›Paper›PMID 30054383›Full record

ArticleJournal of cell science2018

Cell-matrix adhesion controls Golgi organization and function through Arf1 activation in anchorage-dependent cells.

Vibha Singh, Chaitanya Erady, Nagaraj Balasubramanian

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 40 citations in OpenAlex.

  1. Mechanical forces stimulate Golgi export.The Journal of cell biology · 2026
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  9. A transporter's doom or destiny:Frontiers in molecular neuroscience · 2024
    Review
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  11. Review
  12. Review
  13. Crosstalk between mechanotransduction and metabolism.Nature reviews. Molecular cell biology · 2021
    Review
  14. Article
  15. Review
  16. Endomembranes: Unsung Heroes of Mechanobiology?Frontiers in bioengineering and biotechnology · 2020
    Review
  17. Article
  18. Review
  19. 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

3 authors at 1 institution in 1 country.

Vibha SinghIndian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pune, Maharashtra 411008, India.ORCID 0000-0002-1280-6920
Chaitanya EradyIndian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pune, Maharashtra 411008, India.
Nagaraj BalasubramanianIndian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pune, Maharashtra 411008, India nagaraj@iiserpune.ac.in.ORCID 0000-0002-8219-8844
Indian Institute of Science Education and Research Pune · IN

Funding

DBT-Wellcome Trust India Alliance 500238-Z-11-Z
6 · The paper itself

Abstract

Cell-matrix adhesion regulates membrane trafficking controlling anchorage-dependent signaling. While a dynamic Golgi complex can contribute to this pathway, its regulation by adhesion remains unclear. Here we report that loss of adhesion dramatically disorganized the Golgi in mouse and human fibroblast cells. Golgi integrity is restored rapidly upon integrin-mediated re-adhesion to FN and is disrupted by integrin blocking antibody. In suspended cells, the cis, cis-medial and trans-Golgi networks differentially disorganize along the microtubule network but show no overlap with the ER, making this disorganization distinct from known Golgi fragmentation. This pathway is regulated by an adhesion-dependent reduction and recovery of Arf1 activation. Constitutively active Arf1 disrupts this regulation and prevents Golgi disorganization due to loss of adhesion. Adhesion-dependent Arf1 activation regulates its binding to the microtubule minus-end motor protein dynein to control Golgi reorganization, which is blocked by ciliobrevin. Adhesion-dependent Golgi organization controls its function, regulating cell surface glycosylation due to loss of adhesion, which is blocked by constitutively active Arf1. This study, hence, identified integrin-dependent cell-matrix adhesion to be a novel regulator of Arf1 activation, controlling Golgi organization and function in anchorage-dependent cells. This article has an associated First Person interview with the first author of the paper.

Indexed as

ADP-Ribosylation Factor 1AnimalsCell AdhesionCell-Matrix JunctionsCell MembraneCells, CulturedEmbryo, MammalianGolgi ApparatusHumansIntegrinsMiceSignal Transductiontrans-Golgi NetworkADP-Ribosylation Factor 1IntegrinsAdhesionArf1DyneinGlycosylationGolgiIntegrin

Identifiers

PMID30054383
PMCPMC6127727
OpenAlexW2790459574

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.