Evidence map›Paper›PMID 18698806›Full record

ArticleJournal of proteome research2008

Identification of c-Src tyrosine kinase substrates using mass spectrometry and peptide microarrays.

Ramars Amanchy, Jun Zhong, Henrik Molina, Raghothama Chaerkady, Akiko Iwahori, Dario Eluan Kalume, Mads Grønborg, Jos Joore, Leslie Cope, Akhilesh Pandey

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

39 citing papers in PubMed, 67 citations in OpenAlex.

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  11. hnRNP L-mediated RNA switches function as a hypoxia-induced translational regulon.Biochemical and biophysical research communications · 2019
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  13. RBM10: Harmful or helpful-many factors to consider.Journal of cellular biochemistry · 2018
    Review
  14. Article
  15. Article
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  17. Article
  18. Article
  19. Review
  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 1 institution in 1 country.

Ramars AmanchyMcKusick-Nathans Institute of Genetic Medicine and the Departments of Biological Chemistry, Pathology and Oncology, Johns Hopkins University, Baltimore, Maryland 21205, USA.
Jun Zhong
Henrik Molina
Raghothama Chaerkady
Akiko Iwahori
Dario Eluan Kalume
Mads Grønborg
Jos Joore
Leslie Cope
Akhilesh Pandey
University of Southern Denmark · DK

Funding

Translational Research Central ServicesP30CA006973 · NCI · JOHNS HOPKINS UNIVERSITY · PI Rosalie Wollett · 1985 to 2026
$208.6M
TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
Molecular Dissection of Growth Factor Receptor SignalingR01CA106424 · NCI · JOHNS HOPKINS UNIVERSITY · PI PANDEY, AKHILESH · 2005 to 2008
$1.1M
NCI NIH HHS CA106424NCI NIH HHS P30 CA006973NCI NIH HHS P30 CA06973-44NCI NIH HHS R01 CA106424NCRR NIH HHS U54 RR020839
6 · The paper itself

Abstract

c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr --> Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.

Indexed as

Protein Array AnalysisAmino Acid SequenceCell LineHumansMass SpectrometryMolecular Sequence DataPeptidesPhosphorylationsrc-Family KinasesSubstrate SpecificityPeptidessrc-Family Kinases

Identifiers

PMID18698806
PMCPMC2646669
OpenAlexW2054587674

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.