Evidence map›Paper›PMID 34870592›Full record

ArticleeLife2021

Src activates retrograde membrane traffic through phosphorylation of GBF1.

Joanne Chia, Shyi-Chyi Wang, Sheena Wee, David James Gill, Felicia Tay, Srinivasaraghavan Kannan, Chandra S Verma, Jayantha Gunaratne, Frederic A Bard

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. The Critical Role of GALNTs-Regulated O-GalNAc Glycosylation in Cancer Malignancy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  5. Review
  6. GalNAc-Transferases in Cancer.Biomedicines · 2025
    Review
  7. Review
  8. Article
  9. Review
  10. Cells · 2023
    Review
  11. Review
  12. Review
  13. Review
  14. Role of theFrontiers in cell and developmental biology · 2022
    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 at 2 institutions in 2 countries.

Joanne ChiaInstitute of Molecular and Cell Biology, Singapore, Singapore.ORCID 0000-0002-6617-0278
Shyi-Chyi WangInstitute of Molecular and Cell Biology, Singapore, Singapore.
Sheena WeeInstitute of Molecular and Cell Biology, Singapore, Singapore.
David James GillInstitute of Molecular and Cell Biology, Singapore, Singapore.
Felicia TayInstitute of Molecular and Cell Biology, Singapore, Singapore.
Srinivasaraghavan KannanBioinformatics Institute, Singapore, Singapore.
Chandra S VermaBioinformatics Institute, Singapore, Singapore.
Jayantha GunaratneInstitute of Molecular and Cell Biology, Singapore, Singapore.ORCID 0000-0002-5377-6537
Frederic A BardInstitute of Molecular and Cell Biology, Singapore, Singapore.ORCID 0000-0002-3783-4805
Bioengineering Center · RUNational University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Src tyrosine kinase controls cancer-critical protein glycosylation through Golgi to ER relocation of GALNTs enzymes. How Src induces this trafficking event is unknown. Golgi to ER transport depends on the GTP exchange factor (GEF) GBF1 and small GTPase Arf1. Here, we show that Src induces the formation of tubular transport carriers containing GALNTs. The kinase phosphorylates GBF1 on 10 tyrosine residues; two of them, Y876 and Y898, are located near the C-terminus of the Sec7 GEF domain. Their phosphorylation promotes GBF1 binding to the GTPase; molecular modeling suggests partial melting of the Sec7 domain and intramolecular rearrangement. GBF1 mutants defective for these rearrangements prevent binding, carrier formation, and GALNTs relocation, while phosphomimetic GBF1 mutants induce tubules. In sum, Src promotes GALNTs relocation by promoting GBF1 binding to Arf1. Based on residue conservation, similar regulation of GEF-Arf complexes by tyrosine phosphorylation could be a conserved and widespread mechanism.

Indexed as

Endoplasmic ReticulumGolgi ApparatusGuanine Nucleotide Exchange FactorsHumansPhosphorylationProtein Transportsrc-Family KinasesGBF1 protein, humanGuanine Nucleotide Exchange Factorssrc-Family KinasesArf1cell biologyGBF1golgihumanmembrane trafficsignallingSrc

Identifiers

PMID34870592
PMCPMC8727025
OpenAlexW4225455740

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.