Evidence map›Paper›PMID 19592663›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2009

Palmitoylation-dependent plasma membrane transport but lipid raft-independent signaling by linker for activation of T cells.

Matthias Hundt, Yohsuke Harada, Lauren De Giorgio, Natsuko Tanimura, Weiguo Zhang, Amnon Altman

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

32 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Detection of Protein S-Acylation using Acyl-Resin Assisted Capture.Journal of visualized experiments : JoVE · 2020
    Article
  12. Acylation - A New Means to Control Traffic Through the Golgi.Frontiers in cell and developmental biology · 2019
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Rapid and transient palmitoylation of the tyrosine kinase Lck mediates Fas signaling.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Article
  20. Membrane raft association is a determinant of plasma membrane localization.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

6 authors at 3 institutions in 2 countries.

Matthias HundtDivision of Cell Biology, La Jolla Institute for Allergy & Immunology, La Jolla, CA 92037, USA.
Yohsuke Harada
Lauren De Giorgio
Natsuko Tanimura
Weiguo Zhang
Amnon Altman
La Jolla Institute for Immunology · USDuke Medical Center · USTokyo Medical University · JP

Funding

Analysis of adaptor protein (LAT) in TCR signalingR01AI048674 · NIAID · DUKE UNIVERSITY · PI ZHANG, WEIGUO · 2001 to 2011
$3.5M
Regulation of T cell anergy by palmitoyl acyl transferasesR21AI081078 · NIAID · LA JOLLA INSTITUTE FOR IMMUNOLOGY · PI ALTMAN, AMNON · 2009 to 2010
$501k
NIAID NIH HHS AI081078NIAID NIH HHS R01 AI048674NIAID NIH HHS R21 AI081078
6 · The paper itself

Abstract

Linker for activation of T cells (LAT) is a dually palmitoylated transmembrane adaptor protein essential for T cell development and activation. However, whether LAT palmitoylation and/or lipid raft localization are required for its function is controversial. To address this question, we used a combination of biochemical, imaging, and genetic approaches, including LAT retrovirus-transduced mouse T cells and bone marrow chimeric mice. A nonpalmitoylated, non-lipid raft-residing mutant of transmembrane LAT could not reconstitute T cell development in bone marrow chimeric mice. This mutant was absent from the plasma membrane (PM) and was restricted mainly to the Golgi apparatus. A chimeric, nonpalmitoylated LAT protein consisting of the PM-targeting N-terminal sequence of Src kinase and the LAT cytoplasmic domain (Src-LAT) localized as a peripheral membrane protein in the PM, but outside lipid rafts. Nevertheless, Src-LAT restored T cell development and activation. Lastly, monopalmitoylation of LAT on Cys(26) (but not Cys(29)) was required and sufficient for its PM transport and function. Thus, the function of LAT in T cells requires its PM, but not raft, localization, even when expressed as a peripheral membrane protein. Furthermore, LAT palmitoylation functions primarily as a sorting signal required for its PM transport.

Indexed as

Signal TransductionAdaptor Proteins, Signal TransducingAnimalsCell MembraneChimeraLipoylationMembrane MicrodomainsMembrane ProteinsMicePhosphoproteinsProtein Transportsrc-Family KinasesT-LymphocytesAdaptor Proteins, Signal TransducingLat protein, mouseMembrane ProteinsPhosphoproteinssrc-Family Kinases

Identifiers

PMID19592663
PMCPMC2782658
OpenAlexW2113233981

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.