Evidence map›Paper›PMID 20368272›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2010

A threonine-based targeting signal in the human CD1d cytoplasmic tail controls its functional expression.

Jianyun Liu, Daniel Shaji, Sungyoo Cho, Wenjun Du, Jacquelyn Gervay-Hague, Randy R Brutkiewicz

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

22 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Immune evasion of the CD1d/NKT cell axis.Current opinion in immunology · 2018
    Review
  7. Review
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
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  18. Review
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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

6 authors at 2 institutions in 1 country.

Jianyun LiuDepartment of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
Daniel Shaji
Sungyoo Cho
Wenjun Du
Jacquelyn Gervay-Hague
Randy R Brutkiewicz
Indiana University School of MedicineUniversity of California, Davis · US

Funding

Poxvirus Modulation of Immune ResponsesP01AI056097 · NIAID · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI BLUM, JANICE S · 2003 to 2010
$9.9M
Immunology and Infectious Diseases Training ProgramT32AI060519 · NIAID · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI MARK H KAPLAN · 2004 to 2026
$6.0M
CDI Molecules &NKT Cells in Host DefenseR01AI046455 · NIAID · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI BRUTKIEWICZ, RANDY R · 2000 to 2009
$2.8M
Synthesis and Screening of Bioactive GlycolipidsR01GM090262 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GERVAY-HAGUE, JACQUELYN · 2009 to 2012
$1.2M
NIAID NIH HHS P01 AI056097NIAID NIH HHS R01 AI046455NIAID NIH HHS R01 AI46455NIAID NIH HHS T32 AI060519NIGMS NIH HHS R01 GM090262
6 · The paper itself

Abstract

CD1d molecules are MHC class I-like molecules that present lipids to a unique subpopulation of T cells called NKT cells. The cytoplasmic tail of human CD1d possesses a tyrosine-based endosomal targeting motif (YXXZ). As such, these molecules traffic through the endocytic pathway, where it is believed that they are loaded with the antigenic lipid that stimulates NKT cells. In the current study, it was found that the T322 residue in the human CD1d tail is a major signal controlling transport to the cell surface and thus its functional expression. Mimicking the phosphorylation of this residue or removal of the entire cytoplasmic tail negates its ability to regulate CD1d trafficking, resulting in lysosomal targeting and degradation. These results demonstrate an important role of a heretofore unknown signal in the cytoplasmic tail of CD1d that may have relevance to other type I integral membrane proteins that traverse through the endocytic pathway.

Indexed as

Amino Acid MotifsAmino Acid SubstitutionAntigens, CD1dCell LineCell Line, TransformedCells, CulturedCoculture TechniquesCytoplasmEndocytosisGene Expression RegulationGene TargetingHumansMembrane ProteinsNatural Killer T-CellsProtein Structure, TertiaryRecombinant Fusion ProteinsAntigens, CD1dCD1D protein, humanMembrane ProteinsRecombinant Fusion ProteinsThreonine

Identifiers

PMID20368272
PMCPMC2858764
OpenAlexW1584746705

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.