Evidence map›Paper›PMID 22416136›Full record

ArticleThe Journal of biological chemistry2012

Tight complex formation between Cosmc chaperone and its specific client non-native T-synthase leads to enzyme activity and client-driven dissociation.

Rajindra P Aryal, Tongzhong Ju, Richard D Cummings

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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. C1GALT1C1-Associated Mosaic Disorder of Glycosylation in a Female.Journal of inherited metabolic disease · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Science advances · 2021
    Article
  10. Immunoglobulin A Glycosylation and Its Role in Disease.Experientia supplementum (2012) · 2021
    Article
  11. Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021
    Article
  12. Article
  13. Alzheimer's & dementia (New York, N. Y.) · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

3 authors at 1 institution in 1 country.

Rajindra P AryalDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Tongzhong Ju
Richard D Cummings
Emory University · US

Funding

Cosmc - A Novel Molecular Chaperone Regulating O-GlycansR01GM068559 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI CUMMINGS, RICHARD D · 2005 to 2009
$1.2M
NIGMS NIH HHS R01 GM068559
6 · The paper itself

Abstract

The interaction of the endoplasmic reticulum molecular chaperone Cosmc with its specific client T-synthase (Core 1 β1-3-galactosyltransferase) is required for folding of the enzyme and eventual movement of the T-synthase to the Golgi, but the mechanism of interaction is unclear. Here we show that the lumenal domain of recombinant Cosmc directly interacts specifically in either free form or covalently bound to solid supports with denatured T-synthase but not with the active dimeric form of the enzyme. This leads to formation of a relatively stable complex of Cosmc and denatured T-synthase accompanied by formation of reactivated enzyme in an ATP-independent fashion that is not regulated by redox, calcium, pH, or intermolecular disulfide bond formation. The partly refolded and active T-synthase remains tightly bound noncovalently to Cosmc. Dissociation of T-synthase from the complex is promoted by further interactions of the complex with free forms of either native or non-native T-synthase. Taken together, these results demonstrate a novel mechanism in which Cosmc cycles to bind non-native T-synthase, leading to enzyme activity and release in a client-driven process.

Indexed as

AnimalsBiocatalysisBlotting, WesternCell LineGalactosyltransferasesGolgi ApparatusHumansMolecular ChaperonesMultiprotein ComplexesMutationProtein BindingProtein DenaturationProtein FoldingRecombinant ProteinsSolubilityC1GALT1C1 protein, humanC1GALT1 protein, humanGalactosyltransferasesMolecular ChaperonesMultiprotein ComplexesRecombinant Proteins

Identifiers

PMID22416136
PMCPMC3346102
OpenAlexW1993221671

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.