Evidence map›Paper›PMID 20070606›Full record

ArticleTraffic (Copenhagen, Denmark)2010

Mechanisms of function of tapasin, a critical major histocompatibility complex class I assembly factor.

Syed Monem Rizvi, Malini Raghavan

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Atlantic cod (Frontiers in cell and developmental biology · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Distinct assembly profiles of HLA-B molecules.Journal of immunology (Baltimore, Md. : 1950) · 2014
    Article
  15. Article
  16. Review
  17. Article
  18. 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.

Syed Monem RizviDepartment of Microbiology and Immunology, University of Michigan Medical School, 5641 Medical Science Building II, Ann Arbor, MI 48109-5620, USA.
Malini Raghavan
University of Michigan–Ann Arbor · US

Funding

INTERACTIONS &MECHANISMS OF FUNCTION OF THE TAP COMPLEXR01AI044115 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MALINI RAGHAVAN · 1999 to 2026
$9.3M
Interactions and mechanisms of function of the TAP ComplexR56AI044115 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAGHAVAN, MALINI · 2008 to 2008
$386k
NIAID NIH HHS AI-044115NIAID NIH HHS R01 AI044115NIAID NIH HHS R56 AI044115
6 · The paper itself

Abstract

For their efficient assembly in the endoplasmic reticulum (ER), major histocompatibility complex (MHC) class I molecules require the specific assembly factors transporter associated with antigen processing (TAP) and tapasin, as well as generic ER folding factors, including the oxidoreductases ERp57 and protein disulfide isomerase (PDI), and the chaperone calreticulin. TAP transports peptides from the cytosol into the ER. Tapasin promotes the assembly of MHC class I molecules with peptides. The formation of disulfide-linked conjugates of tapasin with ERp57 is suggested to be crucial for tapasin function. Important functional roles are also suggested for the tapasin transmembrane and cytoplasmic domains, sites of tapasin interaction with TAP. We show that interactions of tapasin with both TAP and ERp57 are correlated with strong MHC class I recruitment and assembly enhancement. The presence of the transmembrane/cytosolic regions of tapasin is critical for efficient tapasin-MHC class I binding in interferon-gamma-treated cells, and contributes to an ERp57-independent mode of MHC class I assembly enhancement. A second ERp57-dependent mode of tapasin function correlates with enhanced MHC class I binding to tapasin and calreticulin. We also show that PDI binds to TAP in a tapasin-independent manner, but forms disulfide-linked conjugates with soluble tapasin. Thus, full-length tapasin is important for enhancing recruitment of MHC class I molecules and increasing specificity of tapasin-ERp57 conjugation. Furthermore, tapasin or the TAP/tapasin complex has an intrinsic ability to recruit MHC class I molecules and promote assembly, but also uses generic folding factors to enhance MHC class I recruitment and assembly.

Indexed as

AnimalsATP-Binding Cassette TransportersCalreticulinCHO CellsCricetinaeCricetulusEndoplasmic ReticulumHeLa CellsHistocompatibility Antigens Class IHumansInterferon-gammaMembrane Transport ProteinsProtein BindingProtein Disulfide-IsomerasesProtein FoldingATP-Binding Cassette TransportersCalreticulinHistocompatibility Antigens Class IInterferon-gammaMembrane Transport ProteinsProtein Disulfide-Isomerasestapasintransporter associated with antigen processing (TAP)

Identifiers

PMID20070606
PMCPMC2983092
OpenAlexW2077906780

What OpenQuestion holds

Textmetadata
LicenceTDM
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.