Evidence map›Paper›PMID 22988244›Full record

ArticleThe Journal of biological chemistry2012

Glycosyltransferase-specific Golgi-targeting mechanisms.

Armen Petrosyan, Mohamed F Ali, Pi-Wan Cheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.7field-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

36 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
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  9. Review
  10. The non-canonical mechanism of ER stress-mediated progression of prostate cancer.Journal of experimental & clinical cancer research : CR · 2021
    Article
  11. Adaptation of the Golgi Apparatus in Cancer Cell Invasion and Metastasis.Frontiers in cell and developmental biology · 2021
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Unlocking Golgi: Why Does Morphology Matter?Biochemistry. Biokhimiia · 2019
    Review
  17. Pluronic block copolymers enhance the anti-myeloma activity of proteasome inhibitors.Journal of controlled release : official journal of the Controlled Release Society · 2019
    Article
  18. The Golgin Protein Giantin Regulates Interconnections Between Golgi Stacks.Frontiers in cell and developmental biology · 2019
    Article
  19. Article
  20. 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

3 authors at 2 institutions in 2 countries.

Armen PetrosyanDepartment of Research Service, Veterans Affairs Nebraska-Western Iowa Health Care System, Omaha, Nebraska 68105, USA.
Mohamed F Ali
Pi-Wan Cheng
VA Nebraska Western Iowa Health Care System · USInstitute of Molecular Biology · BG

Funding

BIOSYNTHESIS OF TRACHEAL MUCOUS GLYCOPROTEINSR01HL048282 · NHLBI · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI CHENG, PI-WAN · 1995 to 2010
$2.2M
Control of Mucin Glycan Branching in Membrane-bound and Secreted MucinsR21HL097238 · NHLBI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CHENG, PI-WAN · 2009 to 2010
$385k
Glycosyltransferase Golgi Retention MechanismI01BX000985 · VA · OMAHA VA MEDICAL CENTER · PI CHENG, PI-WAN · 2011 to 2015
–
BLRD VA I01 BX000985NHLBI NIH HHS 1R21HL097238NHLBI NIH HHS 2R01HL48282NHLBI NIH HHS R01 HL048282NHLBI NIH HHS R21 HL097238
6 · The paper itself

Abstract

Glycosylation of secreted and membrane-bound mucins is carried out by glycosyltransferases localized to specific Golgi compartments according to the step in which each enzyme participates. However, the Golgi-targeting mechanisms of these enzymes are not clear. Herein, we investigate the Golgi-targeting mechanisms of core 1 β3 galactosyltransferase (C1GalT1) and core 2 β1,6-N-acetylglucosaminyltransferase-2 or mucus type (C2GnT-M), which participate in the early O-glycosylation steps. siRNAs, co-immunoprecipitation, and confocal fluorescence microscopy were employed to identify the golgins involved in the Golgi docking of vesicular complexes (VCs) that carry these two enzymes. We have found that these VCs use different golgins for docking: C2GnT-M-carrying VC (C2GnT-M-VC) utilizes Giantin, whereas C1GalT1-VC employs GM130-GRASP65 complex. However, in the absence of GRASP65, C1GalT1-VC utilizes GM130-Giantin complex. Also, we have found that these VCs are 1.1-1.2 μm in diameter, specific for each enzyme, and independent of coat protein complex II and I (COPII and COPI). These two fluorescently tagged enzymes exhibit different fluorescence recovery times in the Golgi after photobleaching. Thus, novel enzyme-specific Golgi-targeting mechanisms are employed by glycosyltransferases, and multiple Golgi docking strategies are utilized by C1GalT1.

Indexed as

AutoantigensBlotting, WesternCell Line, TumorCoatomer ProteinGalactosyltransferasesGlycosylationGolgi ApparatusGolgi Matrix ProteinsGreen Fluorescent ProteinsHEK293 CellsHumansLuminescent ProteinsMembrane ProteinsMicroscopy, ConfocalMicroscopy, FluorescenceN-AcetylglucosaminyltransferasesAutoantigensbeta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3C1GALT1 protein, humanCoatomer ProteinGalactosyltransferasesGolgi Matrix ProteinsGolgin subfamily A member 2GORASP1 protein, humanGreen Fluorescent ProteinsLuminescent ProteinsmacrogolginMembrane ProteinsN-AcetylglucosaminyltransferasesRed Fluorescent ProteinVesicular Transport Proteins

Identifiers

PMID22988244
PMCPMC3488040
OpenAlexW2025590149

What OpenQuestion holds

Textmetadata
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.