Evidence map›Paper›PMID 20956537›Full record

ArticleThe Journal of biological chemistry2010

Regulation of Syk by phosphorylation on serine in the linker insert.

Leela L Paris, Jianjie Hu, Jacob Galan, Su Sien Ong, Victoria A Martin, Haiyan Ma, W Andy Tao, Marietta L Harrison, Robert L Geahlen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Feedback Regulation of Syk by Protein Kinase C in Human Platelets.International journal of molecular sciences · 2019
    Article
  6. Review
  7. Article
  8. Article
  9. GThe Journal of biological chemistry · 2017
    Article
  10. Review
  11. Article
  12. Article
  13. Dynamic allostery: linkers are not merely flexible.Structure (London, England : 1993) · 2011
    Review
  14. Article
  15. Review
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

9 authors at 2 institutions in 1 country.

Leela L ParisDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, Indiana 47907, USA.
Jianjie Hu
Jacob Galan
Su Sien Ong
Victoria A Martin
Haiyan Ma
W Andy Tao
Marietta L Harrison
Robert L Geahlen
Purdue University West Lafayette · USCenter for Cancer Research · US

Funding

TYROSINE PROTEIN KINASES AND LYMPHOCYTE ACTIVATIONR01CA037372 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI GEAHLEN, ROBERT L · 1985 to 2011
$3.5M
New Proteomic Technologies for the Analysis of Tyrosine Kinase Signaling PathwaysR01GM088317 · NIGMS · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2010 to 2014
$1.6M
Syk and associated proteins in breast cancerR01CA115465 · NCI · PURDUE UNIVERSITY · PI GEAHLEN, ROBERT L · 2007 to 2011
$1.4M
Acquisition of a High Resolution Orbitrap Mass Spectrometer for Analysis of ProteS10RR025044 · NCRR · PURDUE UNIVERSITY · PI TAO, W. ANDY · 2009 to 2009
$969k
NCI NIH HHS CA037372NCI NIH HHS CA115465NCI NIH HHS R01 CA037372NCI NIH HHS R01 CA115465NCRR NIH HHS S10 RR025044NIGMS NIH HHS R01 GM088317
6 · The paper itself

Abstract

The Syk protein-tyrosine kinase is phosphorylated on multiple tyrosines after the aggregation of the B cell antigen receptor. However, metabolic labeling experiments indicate that Syk is inducibly phosphorylated to an even greater extent on serine after receptor ligation. A combination of phosphopeptide mapping and mass spectrometric analyses indicates that serine 291 is a major site of phosphorylation. Serine 291 lies within a 23-amino acid insert located within the linker B region that distinguishes Syk from SykB and Zap-70. The phosphorylation of serine-291 by protein kinase C enhances the ability of Syk to couple the antigen receptor to the activation of the transcription factors NFAT and Elk-1. Protein interaction studies indicate a role for the phosphorylated linker insert in promoting an interaction between Syk and the chaperone protein, prohibitin.

Indexed as

ets-Domain Protein Elk-1HumansIntracellular Signaling Peptides and ProteinsNFATC Transcription FactorsPeptide MappingPhosphorylationProtein-Tyrosine KinasesReceptors, Antigen, B-CellSerineSyk KinaseU937 CellsZAP-70 Protein-Tyrosine KinaseELK1 protein, humanets-Domain Protein Elk-1Intracellular Signaling Peptides and ProteinsNFATC Transcription FactorsProtein-Tyrosine KinasesReceptors, Antigen, B-CellSerineSyk KinaseSYK protein, humanZAP70 protein, humanZAP-70 Protein-Tyrosine Kinase

Identifiers

PMID20956537
PMCPMC3000966
OpenAlexW2086716801

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.