Evidence map›Paper›PMID 18410729›Full record

ArticleDevelopmental cell2008

Golgi localization of glycosyltransferases requires a Vps74p oligomer.

Karl R Schmitz, Jingxuan Liu, Shiqing Li, Thanuja Gangi Setty, Christopher S Wood, Christopher G Burd, Kathryn M Ferguson

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

111 citing papers in PubMed, 197 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A class of COPI cargo receptors regulates processing of transmembrane proteins by reinforcing their Golgi retention.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Golgi Drivers of Cancer.Sub-cellular biochemistry · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Trafficking and localization of Golgi-residentFrontiers in plant science · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Vesicle trafficking in rice: too little is known.Frontiers in plant science · 2023
    Review

51 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 1 country.

Karl R SchmitzDepartment of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
Jingxuan Liu
Shiqing Li
Thanuja Gangi Setty
Christopher S Wood
Christopher G Burd
Kathryn M Ferguson
University of Pennsylvania · US

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI THORNE, ROBERT E. · 1985 to 2011
$23.8M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
TRAFFICKING BY FYVE DOMAIN EFFECTORS OF PI3 KINASER01GM061221 · NIGMS · YALE UNIVERSITY · PI BURD, CHRISTOPHER G · 2000 to 2016
$5.2M
Analysis of active and inactive EGFR conformationsR01CA112552 · NCI · YALE UNIVERSITY · PI FERGUSON, KATHRYN M · 2005 to 2015
$2.4M
Sorting and Trafficking in the Endosomal SystemR37GM061221 · NIGMS · YALE UNIVERSITY · PI BURD, CHRISTOPHER G · 2017 to 2021
$2.0M
NCI NIH HHS R01 CA112552NCI NIH HHS Y1-CO-1020NCRR NIH HHS P41 RR001646NCRR NIH HHS RR-01646NIGMS NIH HHS GM08275NIGMS NIH HHS GM61221NIGMS NIH HHS R01 GM061221NIGMS NIH HHS R37 GM061221NIGMS NIH HHS T32 GM008275NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

The mechanism of glycosyltransferase localization to the Golgi apparatus is a long-standing question in secretory cell biology. All Golgi glycosyltransferases are type II membrane proteins with small cytosolic domains that contribute to Golgi localization. To date, no protein has been identified that recognizes the cytosolic domains of Golgi enzymes and contributes to their localization. Here, we report that yeast Vps74p directly binds to the cytosolic domains of cis and medial Golgi mannosyltransferases and that loss of this interaction correlates with loss of Golgi localization of these enzymes. We have solved the X-ray crystal structure of Vps74p and find that it forms a tetramer, which we also observe in solution. Deletion of a critical structural motif disrupts tetramer formation and results in loss of Vps74p localization and function. Vps74p is highly homologous to the human GMx33 Golgi matrix proteins, suggesting a conserved function for these proteins in the Golgi enzyme localization machinery.

Indexed as

Protein Structure, QuaternarySaccharomyces cerevisiaeCarrier ProteinsCrystallography, X-RayGlycosylationGlycosyltransferasesGolgi ApparatusHeLa CellsHumansModels, MolecularMolecular ChaperonesMolecular Sequence DataRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsCarrier ProteinsGlycosyltransferasesMolecular ChaperonesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsVps74 protein, S cerevisiae

Identifiers

PMID18410729
PMCPMC2707253
OpenAlexW1989893248

What OpenQuestion holds

Textmetadata
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.