Evidence map›Paper›PMID 31056345›Full record

ArticleDevelopmental cell2019

A GBF1-Dependent Mechanism for Environmentally Responsive Regulation of ER-Golgi Transport.

Mafalda Lopes-da-Silva, Jessica J McCormack, Jemima J Burden, Kimberly J Harrison-Lavoie, Francesco Ferraro, Daniel F Cutler

Open access · hybridAbstract read
In one paragraph

Article in Developmental cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
4.4field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 54 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Mechanical Cues Regulate Cargo Sorting and Export at the Golgi.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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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

6 authors at 2 institutions in 1 country.

Mafalda Lopes-da-SilvaEndothelial Cell Biology Laboratory, MRC Laboratory for Molecular Cell Biology, University College London, London, UK. Electronic address: mafalda.silva@ucl.ac.uk.
Jessica J McCormackEndothelial Cell Biology Laboratory, MRC Laboratory for Molecular Cell Biology, University College London, London, UK.
Jemima J BurdenElectron Microscopy Laboratory, MRC Laboratory for Molecular Cell Biology, University College London, London, UK.
Kimberly J Harrison-LavoieEndothelial Cell Biology Laboratory, MRC Laboratory for Molecular Cell Biology, University College London, London, UK.
Francesco FerraroEndothelial Cell Biology Laboratory, MRC Laboratory for Molecular Cell Biology, University College London, London, UK.
Daniel F CutlerEndothelial Cell Biology Laboratory, MRC Laboratory for Molecular Cell Biology, University College London, London, UK. Electronic address: d.cutler@ucl.ac.uk.
University College London · GBMRC Laboratory for Molecular Cell Biology · GB

Funding

Medical Research Council MC_UU_00012/2Medical Research Council MC_UU_12018/2Medical Research Council MR/K015826/1Medical Research Council MR/M02492X/1
6 · The paper itself

Abstract

How can anterograde membrane trafficking be modulated by physiological cues? A screen of Golgi-associated proteins revealed that the ARF-GEF GBF1 can selectively modulate the ER-Golgi trafficking of prohaemostatic von Willebrand factor (VWF) and extracellular matrix (ECM) proteins in human endothelial cells and in mouse fibroblasts. The relationship between levels of GBF1 and the trafficking of VWF into forming secretory granules confirmed GBF1 is a limiting factor in this process. Further, GBF1 activation by AMPK couples its control of anterograde trafficking to physiological cues; levels of glucose control GBF1 activation in turn modulating VWF trafficking into secretory granules. GBF1 modulates both ER and TGN exit, the latter dramatically affecting the size of the VWF storage organelles, thereby influencing the hemostatic capacity of the endothelium. The role of AMPK as a central integrating element of cellular pathways with intra- and extra-cellular cues can now be extended to modulation of the anterograde secretory pathway.

Indexed as

ADP-Ribosylation Factor 1ADP-Ribosylation FactorsAMP-Activated Protein KinasesAnimalsCells, CulturedEndoplasmic ReticulumFibroblastsGolgi ApparatusGuanine Nucleotide Exchange FactorsHumansHuman Umbilical Vein Endothelial CellsIntracellular MembranesMicePhosphorylationProtein Transportvon Willebrand FactorADP-Ribosylation Factor 1ADP-Ribosylation FactorsAMP-Activated Protein KinasesARF1 protein, humanARF4 protein, humanGBF1 protein, humanGuanine Nucleotide Exchange Factorsvon Willebrand FactorAMPKanterograde traffickingcollagenendothelial cellsGBF1Golgihemostasisorganelle sizesecretionvon Willebrand factor

Identifiers

PMID31056345
PMCPMC6764485
OpenAlexW2942608650

What Socratic 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 Socratic graph.