Evidence map›Paper›PMID 23990450›Full record

ArticleCell stress & chaperones2014

Golgi fragmentation induced by heat shock or inhibition of heat shock proteins is mediated by non-muscle myosin IIA via its interaction with glycosyltransferases.

Armen Petrosyan, Pi-Wan Cheng

Open access · bronzeAbstract read
In one paragraph

Article in Cell stress & chaperones, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  7. Unlocking Golgi: Why Does Morphology Matter?Biochemistry. Biokhimiia · 2019
    Review
  8. Article
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  10. Review
  11. THE IMPACT OF ALCOHOL ON PRO-METASTATIC N-GLYCOSYLATION IN PROSTATE CANCER.Krimskii zhurnal eksperimental'noi i klinicheskoi meditsiny = Kryms'kyi zhurnal eksperymental'noi ta klinichnoi medytsyny = Crimean journal of experimental and clinical medicine · 2018
    Article
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  19. Onco-Golgi: Is Fragmentation a Gate to Cancer Progression?Biochemistry & molecular biology journal
    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

2 authors at 1 institution in 1 country.

Armen PetrosyanDepartment of Research Service, Veterans Administration Nebraska-Western Iowa Health Care System, Omaha, NE, USA.
Pi-Wan Cheng
United States Department of Veterans Affairs · US

Funding

Glycosyltransferase Golgi Retention MechanismI01BX000985 · VA · OMAHA VA MEDICAL CENTER · PI CHENG, PI-WAN · 2011 to 2015
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BLRD VA I01 BX000985
6 · The paper itself

Abstract

The Golgi apparatus is a highly dynamic organelle which frequently undergoes morphological changes in certain normal physiological processes or in response to stress. The mechanisms are largely not known. We have found that heat shock of Panc1 cells expressing core 2 N-acetylglucosaminyltransferase-M (Panc1-C2GnT-M) induces Golgi disorganization by increasing non-muscle myosin IIA (NMIIA)-C2GnT-M complexes and polyubiquitination and proteasomal degradation of C2GnT-M. These effects are prevented by inhibition or knockdown of NMIIA. Also, the speed of Golgi fragmentation induced by heat shock is found to be positively correlated with the levels of C2GnT-M in the Golgi. The results are reproduced in LNCaP cells expressing high levels of two endogenous glycosyltransferases-core 2 N-acetylglucosaminyltransferase-L:1 and β-galactoside:α2-3 sialyltransferase 1. Further, during recovery after heat shock, Golgi reassembly as monitored by a Golgi matrix protein giantin precedes the return of C2GnT-M to the Golgi. The results are consistent with the roles of giantin as a building block of the Golgi architecture and a docking site for transport vesicles carrying glycosyltransferases. In addition, inhibition/depletion of HSP70 or HSP90 in Panc1-C2GnT-M cells also causes an increase of NMIIA-C2GnT-M complexes and NMIIA-mediated Golgi fragmentation but results in accumulation or degradation of C2GnT-M, respectively. These results can be explained by the known functions of these two HSP: participation of HSP90 in protein folding and HSP70 in protein folding and degradation. We conclude that NMIIA is the master regulator of Golgi fragmentation induced by heat shock or inhibition/depletion of HSP70/90.

Indexed as

Heat-Shock Responsebeta-Galactoside alpha-2,3-SialyltransferaseCell Line, TumorCell ShapeCytoplasmGene Knockdown TechniquesGolgi ApparatusHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansN-AcetylglucosaminyltransferasesNonmuscle Myosin Type IIAProtein BindingRNA, Small InterferingSialyltransferasesbeta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-acetylglucosaminyl transferasebeta-Galactoside alpha-2,3-SialyltransferaseHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsN-AcetylglucosaminyltransferasesNonmuscle Myosin Type IIARNA, Small InterferingSialyltransferasesST3GAL1 protein, human

Identifiers

PMID23990450
PMCPMC3933620
OpenAlexW1984847156

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.