Evidence map›Paper›PMID 21918188›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2011

Myeloid differentiation factor-2 interacts with Lyn kinase and is tyrosine phosphorylated following lipopolysaccharide-induced activation of the TLR4 signaling pathway.

Pearl Gray, Jargalsaikhan Dagvadorj, Kathrin S Michelsen, Constantinos Brikos, Altan Rentsendorj, Terrence Town, Timothy R Crother, Moshe Arditi

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Tyrosine phosphorylation in Toll-like receptor signaling.Cytokine & growth factor reviews · 2014
    Review
  12. Article
  13. Identification of macrophage genes responsive to extracellular acidification.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2013
    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

8 authors at 1 institution in 1 country.

Pearl GrayDivision of Pediatric Infectious Diseases and Immunology, Cedars-Sinai Medical Center, Los Angeles, CA 90048, USA.
Jargalsaikhan Dagvadorj
Kathrin S Michelsen
Constantinos Brikos
Altan Rentsendorj
Terrence Town
Timothy R Crother
Moshe Arditi
Cedars-Sinai Medical Center · US

Funding

MOLECULAR PATHOGENESIS OF CHLAMYDIA-INDUCED ATHEROGENESIR01HL066436 · NHLBI · CEDARS-SINAI MEDICAL CENTER · PI ARDITI, MOSHE · 2001 to 2013
$3.6M
MD2 signaling in LPS/TLR4 induced cellular responsesR01AI058128 · NIAID · CEDARS-SINAI MEDICAL CENTER · PI ARDITI, MOSHE · 2004 to 2009
$2.4M
NHLBI NIH HHS HL-66436NHLBI NIH HHS R01 HL066436NIAID NIH HHS AI-058128NIAID NIH HHS R01 AI058128
6 · The paper itself

Abstract

Stimulation with LPS induces tyrosine phosphorylation of numerous proteins involved in the TLR signaling pathway. In this study, we demonstrated that myeloid differentiation factor-2 (MD-2) is also tyrosine phosphorylated following LPS stimulation. LPS-induced tyrosine phosphorylation of MD-2 is specific; it is blocked by the tyrosine kinase inhibitor, herbimycin A, as well as by an inhibitor of endocytosis, cytochalasin D, suggesting that MD-2 phosphorylation occurs during trafficking of MD-2 and not on the cell surface. Furthermore, we identified two possible phospho-accepting tyrosine residues at positions 22 and 131. Mutant proteins in which these tyrosines were changed to phenylalanine had reduced phosphorylation and significantly diminished ability to activate NF-κB in response to LPS. In addition, MD-2 coprecipitated and colocalized with Lyn kinase, most likely in the endoplasmic reticulum. A Lyn-binding peptide inhibitor abolished MD-2 tyrosine phosphorylation, suggesting that Lyn is a likely candidate to be the kinase required for MD-2 tyrosine phosphorylation. Our study demonstrated that tyrosine phosphorylation of MD-2 is important for signaling following exposure to LPS and underscores the importance of this event in mediating an efficient and prompt immune response.

Indexed as

Enzyme-Linked Immunosorbent AssayHEK293 CellsHumansImmunoblottingImmunoprecipitationLipopolysaccharidesLymphocyte Antigen 96Microscopy, FluorescencePhosphotyrosineSignal Transductionsrc-Family KinasesToll-Like Receptor 4LipopolysaccharidesLY96 protein, humanLymphocyte Antigen 96lyn protein-tyrosine kinasePhosphotyrosinesrc-Family KinasesTLR4 protein, humanToll-Like Receptor 4

Identifiers

PMID21918188
PMCPMC3186846
OpenAlexW2098527874

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.