Evidence map›Paper›PMID 20861015›Full record

ArticleThe Journal of biological chemistry2010

Calreticulin controls the rate of assembly of CD1d molecules in the endoplasmic reticulum.

Yajuan Zhu, Wei Zhang, Natacha Veerapen, Gurdyal Besra, Peter Cresswell

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Three-Dimensional Modeling ofAntibodies (Basel, Switzerland) · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Chaperones: needed for both the good times and the bad times.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    Article
  7. Review
  8. Review
  9. Review
  10. Proprotein convertases process Pmel17 during secretion.The Journal of biological chemistry · 2011
    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

5 authors at 3 institutions in 2 countries.

Yajuan ZhuDepartment of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06520-8011, USA.
Wei Zhang
Natacha Veerapen
Gurdyal Besra
Peter Cresswell
University of Birmingham · GBHoward Hughes Medical Institute · USYale University · US

Funding

Molecular Aspects of Human CD1d FunctionsR01AI059167 · NIAID · YALE UNIVERSITY · PI CRESSWELL, PETER · 2004 to 2019
$5.6M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI059167
6 · The paper itself

Abstract

CD1d is an MHC class I-like molecule comprised of a transmembrane glycoprotein (heavy chain) associated with β(2)-microglobulin (β(2)m) that presents lipid antigens to NKT cells. Initial folding of the heavy chain involves its glycan-dependent association with calreticulin (CRT), calnexin (CNX), and the thiol oxidoreductase ERp57, and is followed by assembly with β(2)m to form the heterodimer. Here we show that in CRT-deficient cells CD1d heavy chains convert to β(2)m-associated dimers at an accelerated rate, indicating faster folding of the heavy chain, while the rate of intracellular transport after assembly is unaffected. Unlike the situation with MHC class I molecules, antigen presentation by CD1d is not impaired in the absence of CRT. Instead, there are elevated levels of stable and functional CD1d on the surface of CRT-deficient cells. Association of the heavy chains with the ER chaperones Grp94 and Bip is observed in the absence of CRT, and these may replace CRT in mediating CD1d folding and assembly. ER retention of free CD1d heavy chains is impaired in CRT-deficient cells, allowing their escape and subsequent expression on the plasma membrane. However, these free heavy chains are rapidly internalized and degraded in lysosomes, indicating that β(2)m association is required for the exceptional resistance of CD1d to lysosomal degradation that is normally observed.

Indexed as

AnimalsAntigen PresentationAntigens, CD1dbeta 2-MicroglobulinCalbindin 2CalnexinCell LineCell MembraneEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPGene Expression RegulationHeat-Shock ProteinsHistocompatibility Antigens Class IHumansLipidsLysosomesAntigens, CD1dbeta 2-MicroglobulinCalbindin 2CalnexinCd1d1 protein, mouseCD1D protein, humanEndoplasmic Reticulum Chaperone BiPendoplasminHeat-Shock ProteinsHistocompatibility Antigens Class ILipidsMembrane GlycoproteinsPDIA3 protein, humanPdia3 protein, mouseProtein Disulfide-IsomerasesS100 Calcium Binding Protein G

Identifiers

PMID20861015
PMCPMC2992262
OpenAlexW2018607054

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.