Evidence map›Paper›PMID 34821548›Full record

ArticleeLife2021

Golgi membrane protein Erd1 Is essential for recycling a subset of Golgi glycosyltransferases.

Richa Sardana, Carolyn M Highland, Beth E Straight, Christopher F Chavez, J Christopher Fromme, Scott D Emr

Abstract 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Golgi Drivers of Cancer.Sub-cellular biochemistry · 2026
    Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Role of theFrontiers in cell and developmental biology · 2022
    Review
  14. 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

6 authors.

Richa SardanaDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.ORCID 0000-0001-5861-9648
Carolyn M HighlandDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.ORCID 0000-0003-4029-0113
Beth E StraightDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.
Christopher F ChavezDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.
J Christopher FrommeDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.ORCID 0000-0002-8837-0473
Scott D EmrDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.ORCID 0000-0002-5408-6781

Funding

GTPase Regulation of the Golgi Complex (Diversity Supplement 2023)R35GM136258 · NIGMS · CORNELL UNIVERSITY · PI J Christopher Fromme · 2020 to 2026
$4.0M
NIGMS NIH HHS R35 GM136258
6 · The paper itself

Abstract

Protein glycosylation in the Golgi is a sequential process that requires proper distribution of transmembrane glycosyltransferase enzymes in the appropriate Golgi compartments. Some of the cytosolic machinery required for the steady-state localization of some Golgi enzymes are known but existing models do not explain how many of these enzymes are localized. Here, we uncover the role of an integral membrane protein in yeast, Erd1, as a key facilitator of Golgi glycosyltransferase recycling by directly interacting with both the Golgi enzymes and the cytosolic receptor, Vps74. Loss of Erd1 function results in mislocalization of Golgi enzymes to the vacuole/lysosome. We present evidence that Erd1 forms an integral part of the recycling machinery and ensures productive recycling of several early Golgi enzymes. Our work provides new insights on how the localization of Golgi glycosyltransferases is spatially and temporally regulated, and is finely tuned to the cues of Golgi maturation.

Indexed as

GlycosylationGlycosyltransferasesGolgi ApparatusMembrane ProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsERD1 protein, S cerevisiaeGlycosyltransferasesMembrane ProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae Proteinscell biologycog complexCOG complexcopierd1Erd1glycosylationGlycosylationglycosyl transferaseglycosyltransferasegolgiGolgi recyclinggolph3recyclingvps74Vps74

Identifiers

PMID34821548
PMCPMC8616560

What OpenQuestion holds

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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.