Evidence map›Paper›PMID 25074978›Full record

ArticleScience signaling2014

The COP II adaptor protein TMED7 is required to initiate and mediate the delivery of TLR4 to the plasma membrane.

Ardiyanto Liaunardy-Jopeace, Clare E Bryant, Nicholas J Gay

Abstract read
In one paragraph

Article in Science signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.

  1. TMED family genes and their roles in human diseases.International journal of medical sciences · 2023
    Pooled it
  2. Article
  3. Article
  4. Article
  5. Transcriptomic and Proteomic Insights Into Buffalo Milk Fat Synthesis and the Role of IGFBP4 in BMECs.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Ardiyanto Liaunardy-JopeaceDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK.
Clare E BryantDepartment of Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge CB3 0ES, UK.
Nicholas J GayDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK. njg11@cam.ac.uk.
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H003916/1Medical Research Council G1000133Wellcome Trust 081744Wellcome Trust 100321Wellcome Trust WT081744/Z/06/ZWellcome Trust WT100321/z/12/Z
6 · The paper itself

Abstract

Toll-like receptor 4 (TLR4), the receptor for the bacterial product endotoxin, is subject to multiple points of regulation at the levels of signaling, biogenesis, and trafficking. Dysregulation of TLR4 signaling can cause serious inflammatory diseases, such as sepsis. We found that the p24 family protein TMED7 (transmembrane emp24 protein transport domain containing 7) is required for the trafficking of TLR4 from the endoplasmic reticulum to the cell surface through the Golgi. TMED7 formed a stable complex with the ectodomain of TLR4, an interaction that required the coiled-coil and Golgi dynamics (GOLD) domains, but not the cytosolic, coat protein complex II (COP II) sorting motif, of TMED7. Depletion of TMED7 reduced TLR4 signaling mediated by the adaptor protein MyD88 (myeloid differentiation marker 88), but not that mediated by the adaptor proteins TRIF [Toll-interleukin-1 receptor (TIR) domain-containing adaptor protein inducing interferon-β] and TRAM (TRIF-related adaptor molecule). Truncated forms of TMED7 lacking the COP II sorting motif or the transmembrane domain were mislocalized and resulted in ligand-independent signaling that probably arises from receptors accumulated intracellularly. Together, these results support the hypothesis that p24 proteins perform a quality control step by recognizing correctly folded anterograde cargo, such as TLR4, in early secretory compartments and facilitating the translocation of this cargo to the cell surface.

Indexed as

Amino Acid MotifsAnimalsCell MembraneCytoplasmCytosolEndoplasmic ReticulumFlow CytometryGolgi ApparatusHEK293 CellsHumansInflammationLigandsMicroscopy, ConfocalMicroscopy, FluorescenceMutagenesisMyeloid Differentiation Factor 88LigandsMYD88 protein, humanMyeloid Differentiation Factor 88TLR4 protein, humanTMED7 protein, humanToll-Like Receptor 4Vesicular Transport Proteins

Identifiers

PMID25074978
PMCPMC4685749
OpenAlexW1981093504

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.