Evidence map›Paper›PMID 34943782›Full record

ReviewCells2021

Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation.

Zinia D'Souza, Farhana Taher Sumya, Amrita Khakurel, Vladimir Lupashin

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Putative role of TMEM165 in congenital cardiomyopathies.Frontiers in molecular neuroscience · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Review
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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

4 authors at 1 institution in 1 country.

Zinia D'SouzaDepartment of Physiology and Cell Biology, University of Arkansas for Medical Sciences, 4301 West Markham Street, Little Rock, AR 72205, USA.
Farhana Taher SumyaDepartment of Physiology and Cell Biology, University of Arkansas for Medical Sciences, 4301 West Markham Street, Little Rock, AR 72205, USA.
Amrita KhakurelDepartment of Physiology and Cell Biology, University of Arkansas for Medical Sciences, 4301 West Markham Street, Little Rock, AR 72205, USA.
Vladimir LupashinDepartment of Physiology and Cell Biology, University of Arkansas for Medical Sciences, 4301 West Markham Street, Little Rock, AR 72205, USA.ORCID 0000-0002-2350-1962
University of Arkansas for Medical Sciences · US

Funding

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
NIGMS NIH HHS R01 GM083144
6 · The paper itself

Abstract

The Golgi is the central organelle of the secretory pathway and it houses the majority of the glycosylation machinery, which includes glycosylation enzymes and sugar transporters. Correct compartmentalization of the glycosylation machinery is achieved by retrograde vesicular trafficking as the secretory cargo moves forward by cisternal maturation. The vesicular trafficking machinery which includes vesicular coats, small GTPases, tethers and SNAREs, play a major role in coordinating the Golgi trafficking thereby achieving Golgi homeostasis. Glycosylation is a template-independent process, so its fidelity heavily relies on appropriate localization of the glycosylation machinery and Golgi homeostasis. Mutations in the glycosylation enzymes, sugar transporters, Golgi ion channels and several vesicle tethering factors cause congenital disorders of glycosylation (CDG) which encompass a group of multisystem disorders with varying severities. Here, we focus on the Golgi vesicle tethering and fusion machinery, namely, multisubunit tethering complexes and SNAREs and their role in Golgi trafficking and glycosylation. This review is a comprehensive summary of all the identified CDG causing mutations of the Golgi trafficking machinery in humans.

Indexed as

Adaptor Proteins, Vesicular TransportCongenital Disorders of GlycosylationGlycosylationGolgi ApparatusHomeostasisHumansMutationSecretory PathwaySNARE ProteinsSugarsAdaptor Proteins, Vesicular TransportSNARE ProteinsSugarscongenital disorders of glycosylationglycosylationGolgimultisubunit tethering complexesSNAREs

Identifiers

PMID34943782
PMCPMC8699264
OpenAlexW3215997196

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.