Evidence map›Paper›PMID 25022875›Full record

ArticleMolecular & cellular proteomics : MCP2014

Identification of extracellular signal-regulated kinase 1 (ERK1) direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics.

Liang Xue, Pengcheng Wang, Pianpian Cao, Jian-Kang Zhu, W Andy Tao

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Stable Isotope Phosphate Labelling of Diverse Metabolites is Enabled by a Family ofAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  7. Stable Isotope Phosphate Labelling of Diverse Metabolites is Enabled by a Family ofAngewandte Chemie (International ed. in English) · 2022
    Article
  8. Review
  9. Review
  10. Mapping proteome-wide targets of protein kinases in plant stress responses.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Molecular Basis of the Mechanisms Controlling MASTL.Molecular & cellular proteomics : MCP · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Estimating the Efficiency of Phosphopeptide Identification by Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017
    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

5 authors at 1 institution in 1 country.

Liang XueFrom the ‡Departments of Biochemistry.
Pengcheng Wang§Horticulture and Landscape Architecture.
Pianpian Cao¶Mathematics.
Jian-Kang ZhuFrom the ‡Departments of Biochemistry, §Horticulture and Landscape Architecture.
W Andy TaoFrom the ‡Departments of Biochemistry, ‖Medicinal Chemistry and Molecular Pharmacology, **Chemistry, and ‡‡Purdue University Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907 watao@purdue.edu.
Purdue University West Lafayette · US

Funding

CALCIUM SIGNALING--INTRACELL ION HOMEOSTASIS REGULATIONR01GM059138 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI ZHU, JIAN-KANG · 1999 to 2015
$4.4M
New Proteomic Technologies for the Analysis of Tyrosine Kinase Signaling PathwaysR01GM088317 · NIGMS · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2010 to 2014
$1.6M
NIGMS NIH HHS GM088317NIGMS NIH HHS R01 GM059138NIGMS NIH HHS R01 GM088317
6 · The paper itself

Abstract

Kinase mediated phosphorylation signaling is extensively involved in cellular functions and human diseases, and unraveling phosphorylation networks requires the identification of substrates targeted by kinases, which has remained challenging. We report here a novel proteomic strategy to identify the specificity and direct substrates of kinases by coupling phosphoproteomics with a sensitive stable isotope labeled kinase reaction. A whole cell extract was moderately dephosphorylated and subjected to in vitro kinase reaction under the condition in which (18)O-ATP is the phosphate donor. The phosphorylated proteins are then isolated and identified by mass spectrometry, in which the heavy phosphate (+85.979 Da) labeled phosphopeptides reveal the kinase specificity. The in vitro phosphorylated proteins with heavy phosphates are further overlapped with in vivo kinase-dependent phosphoproteins for the identification of direct substrates with high confidence. The strategy allowed us to identify 46 phosphorylation sites on 38 direct substrates of extracellular signal-regulated kinase 1, including multiple known substrates and novel substrates, highlighting the ability of this high throughput method for direct kinase substrate screening.

Indexed as

Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAdenosine TriphosphateApoptosis Regulatory ProteinsArabidopsisCell LineCytoskeletal ProteinsExtracellular Signal-Regulated MAP KinasesGTP-Binding Protein RegulatorsHEK293 CellsHumansIsotope LabelingMAP Kinase Signaling SystemPhosphorylationProteomicsrho GTP-Binding ProteinsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAdenosine TriphosphateApoptosis Regulatory ProteinsBAG3 protein, humanCDC42EP4 protein, humanCytoskeletal ProteinsEPN2 protein, humanExtracellular Signal-Regulated MAP KinasesGTP-Binding Protein Regulatorsperiodate-oxidized adenosine 5'-triphosphaterho GTP-Binding ProteinsRNA-Binding Proteins

Identifiers

PMID25022875
PMCPMC4223502
OpenAlexW1966304758

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.