Evidence map›Paper›PMID 21728379›Full record

ArticleJournal of proteome research2011

The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.

Li Yang, Bhavapriya Vaitheesvaran, Kirsten Hartil, Alan J Robinson, Michael R Hoopmann, Jimmy K Eng, Irwin J Kurland, James E Bruce

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 81 citations in OpenAlex.

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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 4 institutions in 2 countries.

Li YangDepartment of Chemistry, Washington State University, Pullman, Washington 99164, USA.
Bhavapriya Vaitheesvaran
Kirsten Hartil
Alan J Robinson
Michael R Hoopmann
Jimmy K Eng
Irwin J Kurland
James E Bruce
Albert Einstein College of Medicine · USUniversity of Washington · USMRC Mitochondrial Biology Unit · GBWashington State University · US

Funding

Stable Isotope and Metabolomics CoreP60DK020541 · NIDDK · YESHIVA UNIVERSITY · PI PESSIN, JEFFREY E. · 1986 to 2014
$29.8M
Stem Cell-Based Therapies for Radiation-Induced Gastrointestinal Sydrome (RIGS)U19AI091175 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI GUHA, CHANDAN · 2010 to 2014
$13.1M
Quantitation of protein interactions in cancer cellsR01GM086688 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2009 to 2019
$4.2M
Hepatic Insuling Action: Role of the Pentose CycleR01DK058132 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KURLAND, IRWIN JACK · 2002 to 2011
$3.4M
An LC-FTICR Mass Spectrometer for Proteomics and Metabolomics ResearchS10RR025107 · NCRR · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2008 to 2008
$990k
New Technology for Protein Interaction Network and Topology AnalysisR01RR023334 · NCRR · WASHINGTON STATE UNIVERSITY · PI BRUCE, JAMES EDWARD · 2007 to 2009
$750k
Medical Research Council MC_U105674181NCRR NIH HHS R01 RR023334NCRR NIH HHS R01RR023334NCRR NIH HHS S10 RR025107NCRR NIH HHS S10RR025107NIAID NIH HHS U19 AI091175NIAID NIH HHS U19AI091175-01NIDDK NIH HHS DK58132-01A2NIDDK NIH HHS P60 DK020541NIDDK NIH HHS P60DK020541NIDDK NIH HHS R01 DK058132NIGMS NIH HHS R01 GM086688NIGMS NIH HHS R01GM086688
6 · The paper itself

Abstract

The elucidation of extra-nuclear lysine acetylation has been of growing interest, as the cosubstrate for acetylation, acetyl CoA, is at a key metabolic intersection. Our hypothesis was that mitochondrial and cytoplasmic protein acetylation may be part of a fasted/re-fed feedback control system for the regulation of the metabolic network in fuel switching, where acetyl CoA would be provided by fatty acid oxidation, or glycolysis, respectively. To test this, we characterized the mitochondrial and cytoplasmic acetylome in various organs that have a high metabolic rate relative to their mass, and/or switch fuels, under fasted and re-fed conditions (brain, kidney, liver, skeletal muscle, heart muscle, white and brown adipose tissues). Using immunoprecipitation, coupled with LC-MS/MS label free quantification, we show there is a dramatic variation in global quantitative profiles of acetylated proteins from different organs. In total, 733 acetylated peptides from 337 proteins were identified and quantified, out of which 31 acetylated peptides from the metabolic proteins that may play organ-specific roles were analyzed in detail. Results suggest that fasted/re-fed acetylation changes coordinated by organ-specific (de)acetylases in insulin-sensitive versus -insensitive organs may underlie fuel use and switching. Characterization of the tissue-specific acetylome should increase understanding of metabolic conditions wherein normal fuel switching is disrupted, such as in Type II diabetes.

Indexed as

AcetylationAcetyl Coenzyme AAmino Acid SequenceAnimalsChromatography, LiquidCytoplasmEnergy MetabolismFastingImmunoprecipitationLysineMaleMetabolic Networks and PathwaysMiceMice, Inbred StrainsMitochondrial ProteinsMolecular ChaperonesAcetyl Coenzyme ALysineMitochondrial ProteinsMolecular ChaperonesPeptide FragmentsProteinsProteome

Identifiers

PMID21728379
PMCPMC3204869
OpenAlexW2073459416

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.