Evidence map›Paper›PMID 27044110›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Mass-tag labeling reveals site-specific and endogenous levels of protein S-fatty acylation.

Avital Percher, Srinivasan Ramakrishnan, Emmanuelle Thinon, Xiaoqiu Yuan, Jacob S Yount, Howard C Hang

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
10.8field-weighted citation impact, top 1% 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

108 citing papers in PubMed, 176 citations in OpenAlex.

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48 more citing papers are in PubMed but not listed here.

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.

Avital PercherLaboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065;
Srinivasan RamakrishnanLaboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065;
Emmanuelle ThinonLaboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065;
Xiaoqiu YuanLaboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065;
Jacob S YountLaboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065; Department of Microbial Infection and Immunity, Center for Microbial Interface Biology, The Ohio State University, Columbus, OH 43210 yount.37@osu.edu hhang@rockefeller.edu.
Howard C HangLaboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065; yount.37@osu.edu hhang@rockefeller.edu.
Rockefeller University · USThe Ohio State University · US

Funding

Studies on Protein LipidationR01GM087544 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI HANG, HOWARD C · 2010 to 2023
$4.4M
Mechanistic analysis of a posttranslationally modified innate antiviral effectorR00AI095348 · NIAID · OHIO STATE UNIVERSITY · PI YOUNT, JACOB · 2013 to 2014
$494k
Molecular Control of IFITM3 in Restricting Influenza Virus InfectionR56AI114826 · NIAID · OHIO STATE UNIVERSITY · PI YOUNT, JACOB · 2015 to 2015
$366k
NIAID NIH HHS R00 AI095348NIAID NIH HHS R00AI095348NIAID NIH HHS R56 AI114826NIAID NIH HHS R56AI114826NIGMS NIH HHS R01 GM087544NIGMS NIH HHS R01GM087544
6 · The paper itself

Abstract

Fatty acylation of cysteine residues provides spatial and temporal control of protein function in cells and regulates important biological pathways in eukaryotes. Although recent methods have improved the detection and proteomic analysis of cysteine fatty (S-fatty) acylated proteins, understanding how specific sites and quantitative levels of this posttranslational modification modulate cellular pathways are still challenging. To analyze the endogenous levels of protein S-fatty acylation in cells, we developed a mass-tag labeling method based on hydroxylamine-sensitivity of thioesters and selective maleimide-modification of cysteines, termed acyl-PEG exchange (APE). We demonstrate that APE enables sensitive detection of protein S-acylation levels and is broadly applicable to different classes of S-palmitoylated membrane proteins. Using APE, we show that endogenous interferon-induced transmembrane protein 3 is S-fatty acylated on three cysteine residues and site-specific modification of highly conserved cysteines are crucial for the antiviral activity of this IFN-stimulated immune effector. APE therefore provides a general and sensitive method for analyzing the endogenous levels of protein S-fatty acylation and should facilitate quantitative studies of this regulated and dynamic lipid modification in biological systems.

Indexed as

AcylationAnimalsCysteineFatty AcidsMass SpectrometryMembrane ProteinsMiceProtein Processing, Post-TranslationalStaining and LabelingCysteineFatty AcidsMembrane Proteinsfatty-acylationIFITM3influenza viruspalmitoylationPEGylation

Identifiers

PMID27044110
PMCPMC4843475
OpenAlexW2319428081

What OpenQuestion holds

Textmetadata
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.