Evidence map›Paper›PMID 31870253›Full record

ReviewBiochemistry. Biokhimiia2019

Unlocking Golgi: Why Does Morphology Matter?

A Petrosyan

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry. Biokhimiia, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
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  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. The non-canonical mechanism of ER stress-mediated progression of prostate cancer.Journal of experimental & clinical cancer research : CR · 2021
    Article
  17. Article
  18. Review
  19. The Role of GM130 in Nervous System Diseases.Frontiers in neurology · 2021
    Review
  20. Global view of human protein glycosylation pathways and functions.Nature reviews. Molecular cell biology · 2020
    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

1 author at 1 institution in 1 country.

A PetrosyanCollege of Medicine, Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA. apetrosyan@unmc.edu.
University of Nebraska–Lincoln · US

Funding

Targeted mass spectrometry approaches to understand CART processing and recepter interactionsP20GM113126 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI GUO, JIANTAO · 2016 to 2025
$20.8M
The role for alcohol-induced Golgi disorganization in the progression of prostate cancerR01AA027242 · NIAAA · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI PETROSYAN, ARMEN · 2019 to 2023
$1.7M
Alcohol effect on Golgi morphology and functionK01AA022979 · NIAAA · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI PETROSYAN, ARMEN · 2014 to 2018
$544k
NIAAA NIH HHS K01 AA022979NIAAA NIH HHS R01 AA027242NIGMS NIH HHS P20 GM113126
6 · The paper itself

Abstract

The mammalian Golgi apparatus is a highly dynamic organelle, which is normally localized in the juxtanuclear space and plays an essential role in the regulation of cellular homeostasis. While posttranslational modification of cargo is mediated by the resident enzymes (glycosyltransferases, glycosidases, and kinases), the ribbon structure of Golgi and its cisternal stacking mostly rely on the cooperation of coiled-coil matrix golgins. Among them, giantin, GM130, and GRASPs are unique, because they form a tripartite complex and serve as Golgi docking sites for cargo delivered from the endoplasmic reticulum (ER). Golgi undergoes significant disorganization in many pathologies associated with a block of the ER-to-Golgi or intra-Golgi transport, including cancer, different neurological diseases, alcoholic liver damage, ischemic stress, viral infections, etc. In addition, Golgi fragments during apoptosis and mitosis. Here, we summarize and analyze clinically relevant observations indicating that Golgi fragmentation is associated with the selective loss of Golgi residency for some enzymes and, conversely, with the relocation of some cytoplasmic proteins to the Golgi. The central concept is that ER and Golgi stresses impair giantin docking site but have no impact on the GM130-GRASP65 complex, thus inducing mislocalization of giantin-sensitive enzymes only. This cardinally changes the processing of proteins by eliminating the pathways controlled by the missing enzymes and by activating the processes now driven by the GM130-GRASP65-dependent proteins. This type of Golgi disorganization is different from the one induced by the cytoskeleton alteration, which despite Golgi de-centralization, neither impairs function of golgins nor alters trafficking.

Indexed as

AnimalsAutoantigensBinding SitesCarrier ProteinsEndoplasmic ReticulumEndoplasmic Reticulum StressGolgi ApparatusHumansMembrane ProteinsNeoplasmsProtein TransportAutoantigensCarrier ProteinsGolgin subfamily A member 2Membrane Proteinstamalin protein, human

Identifiers

PMID31870253
PMCPMC7291852
OpenAlexW2996446000

What Socratic holds

Textmetadata
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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 Socratic graph.