Evidence map›Paper›PMID 25978619›Full record

ArticlePloS one2015

Quantitative Profiling of Lysine Acetylation Reveals Dynamic Crosstalk between Receptor Tyrosine Kinases and Lysine Acetylation.

Bryan D Bryson, Forest M White

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 14 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

2 authors at 1 institution in 1 country.

Bryan D BrysonDepartment of Biological Engineering, Massachusetts Institute of Technology (MIT), Cambridge, Massachusetts, United States of America; David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology (MIT), Cambridge, Massachusetts, United States of America.
Forest M WhiteDepartment of Biological Engineering, Massachusetts Institute of Technology (MIT), Cambridge, Massachusetts, United States of America; David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology (MIT), Cambridge, Massachusetts, United States of America.
Massachusetts Institute of Technology · US

Funding

VIRUS PRODUCTION COREP30CA014051 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI MATTHEW G. VANDER HEIDEN · 1985 to 2026
$93.9M
Tumor Cell Networks CenterU54CA112967 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LAUFFENBURGER, DOUGLAS A · 2004 to 2015
$26.2M
Vanderbilt Proteome Characterization CenterU24CA159988 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI LIEBLER, DANIEL C · 2011 to 2016
$13.9M
Systems Biology of Insulin ResistanceR24DK090963 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI DAVIS, ROGER J. · 2011 to 2014
$8.4M
Quantitative Analysis of Epidermal Growth Factor Receptor Signaling NetworksR01CA118705 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WHITE, FOREST M · 2008 to 2012
$1.8M
NCI NIH HHS P30 CA014051NCI NIH HHS P30CA14051NCI NIH HHS R01 CA118705NCI NIH HHS R01CA118705NCI NIH HHS U24 CA159988NCI NIH HHS U24CA159988NCI NIH HHS U54 CA112967NCI NIH HHS U54CA112967NIDDK NIH HHS R24 DK090963NIDDK NIH HHS R24DK090963
6 · The paper itself

Abstract

Lysine acetylation has been primarily investigated in the context of transcriptional regulation, but a role for acetylation in mediating other cellular responses has emerged. Multiple studies have described global lysine acetylation profiles for particular biological states, but none to date have investigated the temporal dynamics regulating cellular response to perturbation. Reasoning that lysine acetylation may be altered in response to growth factors, we implemented quantitative mass spectrometry-based proteomics to investigate the temporal dynamics of lysine acetylation in response to growth factor stimulation in cultured carcinoma cell lines. We found that lysine acetylation changed rapidly in response to activation of several different receptor tyrosine kinases by their respective ligands. To uncover the effects of lysine acetylation dynamics on tyrosine phosphorylation signaling networks, cells were treated with an HDAC inhibitor. This short-term pharmacological inhibition of histone deacetylase activity modulated signaling networks involving phosphorylated tyrosine and thereby altered the response to receptor tyrosine kinase activation. This result highlights the interconnectivity of lysine acetylation and tyrosine phosphorylation signaling networks and suggests that HDAC inhibition may influence cellular responses by affecting both types of post-translational modifications.

Indexed as

AcetylationBlotting, WesternCell Line, TumorEpidermal Growth FactorHep G2 CellsHistone Deacetylase InhibitorsHumansImmunoprecipitationInsulinInsulin-Like Growth Factor ILysineMass SpectrometryReceptor Protein-Tyrosine KinasesSignal TransductionEpidermal Growth FactorHistone Deacetylase InhibitorsInsulinInsulin-Like Growth Factor ILysineReceptor Protein-Tyrosine Kinases

Identifiers

PMID25978619
PMCPMC4433260
OpenAlexW1850463748

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.