Evidence map›Paper›PMID 18337472›Full record

ArticleMolecular biology of the cell2008

Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules.

Breanna S Ireland, Ulf Brockmeier, Christopher M Howe, Tim Elliott, David B Williams

RetractedOpen access · greenAbstract readRetracted Publication
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

23 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Genetic ablation of N-linked glycosylation reveals two key folding pathways for R345W fibulin-3, a secreted protein associated with retinal degeneration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  4. Review
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  6. Article
  7. The Ca2+ pumps of the endoplasmic reticulum and Golgi apparatus.Cold Spring Harbor perspectives in biology · 2011
    Review
  8. Essential glycan-dependent interactions optimize MHC class I peptide loading.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. ER Stress and Iron Homeostasis: A New Frontier for the UPR.Biochemistry research international · 2011
    Article
  14. Article
  15. Article
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  19. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Breanna S IrelandDepartment of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Ulf Brockmeier
Christopher M Howe
Tim Elliott
David B Williams
University of Toronto · CAUniversity of Southampton · GB

Funding

Cancer Research UK 10601
6 · The paper itself

Abstract

Calreticulin is a molecular chaperone of the endoplasmic reticulum that uses both a lectin site specific for Glc(1)Man(5-9)GlcNAc(2) oligosaccharides and a polypeptide binding site to interact with nascent glycoproteins. The latter mode of substrate recognition is controversial. To examine the relevance of polypeptide binding to protein folding in living cells, we prepared lectin-deficient mutants of calreticulin and examined their abilities to support the assembly and quality control of mouse class I histocompatibility molecules. In cells lacking calreticulin, class I molecules exhibit inefficient loading of peptide ligands, reduced cell surface expression and aberrantly rapid export from the endoplasmic reticulum. Remarkably, expression of calreticulin mutants that are completely devoid of lectin function fully complemented all of the class I biosynthetic defects. We conclude that calreticulin can use nonlectin-based modes of substrate interaction to effect its chaperone and quality control functions on class I molecules in living cells. Furthermore, pulse-chase coimmunoisolation experiments revealed that lectin-deficient calreticulin bound to a similar spectrum of client proteins as wild-type calreticulin and dissociated with similar kinetics, suggesting that lectin-independent interactions are commonplace in cells and that they seem to be regulated during client protein maturation.

Indexed as

AnimalsAntigen PresentationCalreticulinCell MembraneEndoplasmic ReticulumFibroblastsGolgi ApparatusHistocompatibility Antigens Class IIntracellular SpaceKineticsMiceMolecular ChaperonesMutationOvalbuminPeptidesPhenotypeCalreticulinHistocompatibility Antigens Class IMolecular ChaperonesOvalbuminPeptides

Identifiers

PMID18337472
PMCPMC2397311
OpenAlexW2165512405

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.