Evidence map›Paper›PMID 34161137›Full record

ArticleMolecular biology of the cell2021

The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery.

Amrita Khakurel, Tetyana Kudlyk, Juan S Bonifacino, Vladimir V Lupashin

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. GARP Complex in Golgi Physiology.Sub-cellular biochemistry · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Role of GARP Vesicle Tethering Complex in Golgi Physiology.International journal of molecular sciences · 2023
    Review
  15. Article
  16. Generation and Analysis of hTERT-RPE1 VPS54 Knock-Out and Rescued Cell Lines.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  17. Review
  18. Article
  19. Article
  20. 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

4 authors.

Amrita KhakurelUniversity of Arkansas for Medical Sciences, Department of Physiology and Cell Biology, Little Rock, AR 72205.
Tetyana KudlykUniversity of Arkansas for Medical Sciences, Department of Physiology and Cell Biology, Little Rock, AR 72205.
Juan S BonifacinoNeurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
Vladimir V LupashinUniversity of Arkansas for Medical Sciences, Department of Physiology and Cell Biology, Little Rock, AR 72205.

Funding

Protein Trafficking In The Endosomal-Lysosomal SystemZIAHD001607 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 2009 to 2025
$48.3M
Characterization of mammalian COG complex-interacting intra-Golgi trafficking macR01GM083144 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI VLADIMIR V LUPASHIN · 2008 to 2026
$6.5M
Super-Resolution Light Microscope at University of Arkansas for Medical SciencesS10OD018065 · OD · UNIV OF ARKANSAS FOR MED SCIS · PI STORRIE, BRIAN · 2015 to 2015
$600k
Intramural NIH HHS ZIA HD001607NIGMS NIH HHS R01 GM083144NIH HHS S10 OD018065
6 · The paper itself

Abstract

The Golgi complex is a central hub for intracellular protein trafficking and glycosylation. Steady-state localization of glycosylation enzymes is achieved by a combination of mechanisms involving retention and recycling, but the machinery governing these mechanisms is poorly understood. Herein we show that the Golgi-associated retrograde protein (GARP) complex is a critical component of this machinery. Using multiple human cell lines, we show that depletion of GARP subunits impairs Golgi modification of N- and O-glycans and reduces the stability of glycoproteins and Golgi enzymes. Moreover, GARP-knockout (KO) cells exhibit reduced retention of glycosylation enzymes in the Golgi. A RUSH assay shows that, in GARP-KO cells, the enzyme beta-1,4-galactosyltransferase 1 is not retained at the Golgi complex but instead is missorted to the endolysosomal system. We propose that the endosomal system is part of the trafficking itinerary of Golgi enzymes or their recycling adaptors and that the GARP complex is essential for recycling and stabilization of the Golgi glycosylation machinery. [Media: see text].

Indexed as

Cytoplasmic VesiclesEndosomesGlycosylationGolgi ApparatusHeLa CellsHumansLysosomesMembrane ProteinsProtein Transporttrans-Golgi NetworkVesicular Transport ProteinsGOLPH3 protein, humanMembrane ProteinsVesicular Transport ProteinsVPS53 protein, humanVPS54 protein, human

Identifiers

PMID34161137
PMCPMC8351751

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.