Evidence map›Paper›PMID 25371237›Full record

ArticleBMC biology2014

Chemoproteomics reveals Toll-like receptor fatty acylation.

Nicholas M Chesarino, Jocelyn C Hach, James L Chen, Balyn W Zaro, Murugesan Vs Rajaram, Joanne Turner, Larry S Schlesinger, Matthew R Pratt, Howard C Hang, Jacob S Yount

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
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

56 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. ProteinJournal of pharmaceutical analysis · 2026
    Review
  4. Review
  5. Article
  6. ZDHHC5 and ZDHHC14 promote depression via the mediation of double-negative T cells.Mammalian genome : official journal of the International Mammalian Genome Society · 2025
    Article
  7. Review
  8. Review
  9. Article
  10. Context-dependent roles of palmitoylation in acute respiratory distress syndrome: integrating inflammation, cell death and repair.European respiratory review : an official journal of the European Respiratory Society · 2025
    Review
  11. Review
  12. Palmitoylation in cardiovascular diseases: Molecular mechanism and therapeutic potential.International journal of cardiology. Heart & vasculature · 2025
    Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Unconventional posttranslational modification in innate immunity.Cellular and molecular life sciences : CMLS · 2024
    Review
  18. Article
  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

10 authors at 4 institutions in 1 country.

Nicholas M ChesarinoDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, The Ohio State University, Columbus, OH, 43210, USA. Chesarino.1@osu.edu.
Jocelyn C HachDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, The Ohio State University, Columbus, OH, 43210, USA. hach.6@osu.edu.
James L ChenBiomedical Informatics, Internal Medicine in the Division of Medical Oncology, The Ohio State University, Columbus, OH, 43210, USA. James.Chen@osumc.edu.
Balyn W ZaroDepartments of Chemistry and Molecular and Computational Biology, University of Southern California, Los Angeles, CA, 90089, USA. balynzaro@gmail.com.
Murugesan Vs RajaramDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, The Ohio State University, Columbus, OH, 43210, USA. Murugesan.Rajaram@osumc.edu.
Joanne TurnerDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, The Ohio State University, Columbus, OH, 43210, USA. Joanne.Turner@osumc.edu.
Larry S SchlesingerDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, The Ohio State University, Columbus, OH, 43210, USA. larry.schlesinger@osumc.edu.
Matthew R PrattDepartments of Chemistry and Molecular and Computational Biology, University of Southern California, Los Angeles, CA, 90089, USA. matthew.pratt@usc.edu.
Howard C HangLaboratory of Chemical Biology and Microbial Pathogenesis, Rockefeller University, New York, NY, 10065, USA. hhang@rockefeller.edu.
Jacob S YountDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, The Ohio State University, Columbus, OH, 43210, USA. yount.37@osu.edu.
The Ohio State University · USInterface (United States) · USUniversity of Southern California · USRockefeller University · US

Funding

Studies on Protein LipidationR01GM087544 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI HANG, HOWARD C · 2010 to 2023
$4.4M
Integrative Training in Biomedical SystemsT32GM068412 · NIGMS · OHIO STATE UNIVERSITY · PI PARVIN, JEFFREY D · 2005 to 2020
$2.4M
Mechanistic analysis of a posttranslationally modified innate antiviral effectorR00AI095348 · NIAID · OHIO STATE UNIVERSITY · PI YOUNT, JACOB · 2013 to 2014
$494k
NIAID NIH HHS R00 AI095348NIAID NIH HHS R00AI095348NIGMS NIH HHS R01 GM087544NIGMS NIH HHS R01GM087544NIGMS NIH HHS T32 GM068412NIGMS NIH HHS T32GM068412
6 · The paper itself

Abstract

backgroundPalmitoylation is a 16-carbon lipid post-translational modification that increases protein hydrophobicity. This form of protein fatty acylation is emerging as a critical regulatory modification for multiple aspects of cellular interactions and signaling. Despite recent advances in the development of chemical tools for the rapid identification and visualization of palmitoylated proteins, the palmitoyl proteome has not been fully defined. Here we sought to identify and compare the palmitoylated proteins in murine fibroblasts and dendritic cells.

resultsA total of 563 putative palmitoylation substrates were identified, more than 200 of which have not been previously suggested to be palmitoylated in past proteomic studies. Here we validate the palmitoylation of several new proteins including Toll-like receptors (TLRs) 2, 5 and 10, CD80, CD86, and NEDD4. Palmitoylation of TLR2, which was uniquely identified in dendritic cells, was mapped to a transmembrane domain-proximal cysteine. Inhibition of TLR2 S-palmitoylation pharmacologically or by cysteine mutagenesis led to decreased cell surface expression and a decreased inflammatory response to microbial ligands.

conclusionsThis work identifies many fatty acylated proteins involved in fundamental cellular processes as well as cell type-specific functions, highlighting the value of examining the palmitoyl proteomes of multiple cell types. S-palmitoylation of TLR2 is a previously unknown immunoregulatory mechanism that represents an entirely novel avenue for modulation of TLR2 inflammatory activity.

Indexed as

LipoylationAcylationAnimalsB7-2 AntigenCell MembraneCells, CulturedClick ChemistryComputational BiologyDendritic CellsFibroblastsHEK293 CellsHumansInterferon-alphaLigandsMiceNF-kappa BB7-2 AntigenCd86 protein, mouseInterferon-alphaLigandsNF-kappa BProteomeTLR2 protein, humanToll-Like Receptor 2

Identifiers

PMID25371237
PMCPMC4240870
OpenAlexW2090883317

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.