Evidence map›Paper›PMID 12417718›Full record

ArticleMolecular and cellular biology2002

Phosphorylation of Tyr342 in the linker region of Syk is critical for Fc epsilon RI signaling in mast cells.

Juan Zhang, Elsa Berenstein, Reuben P Siraganian

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

22 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. TULA Proteins in Men, Mice, Hens, and Lice: Welcome to the Family.International journal of molecular sciences · 2023
    Review
  4. Review
  5. TULA-Family Regulators of Platelet Activation.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. DJ-1 regulates mast cell activation and IgE-mediated allergic responses.The Journal of allergy and clinical immunology · 2013
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  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

3 authors at 2 institutions in 1 country.

Juan ZhangReceptors and Signal Transduction Section, Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 20892, USA. lzhang@didr.nidcr.nih.gov
Elsa Berenstein
Reuben P Siraganian
National Institutes of Health · USNational Institute of Dental and Craniofacial Research · US

Funding

Signal Transduction In Mast CellsZ01DE000696 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI SIRAGANIAN, REUBEN P. · 1999 to 2008
$3.8M
MOLECULES INVOLVED IN RECEPTOR MEDIATEDN01DE062614 · NIDCR · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI BILLINGSLEY, MELVIN · 1996 to 2000
$0k
NIDCR NIH HHS N01-DE-62614
6 · The paper itself

Abstract

The linker region of Syk and ZAP70 tyrosine kinases plays an important role in regulating their function. There are three conserved tyrosines in this linker region; Tyr317 of Syk and its equivalent residue in ZAP70 were previously shown to negatively regulate the function of Syk and ZAP70. Here we studied the roles of the other two tyrosines, Tyr342 and Tyr346 of Syk, in Fc epsilon RI-mediated signaling. Antigen stimulation resulted in Tyr342 phosphorylation in mast cells. Syk with Y342F mutation failed to reconstitute Fc epsilon RI-initiated histamine release. In the Syk Y342F-expressing cells there was dramatically impaired receptor-induced phosphorylation of multiple signaling molecules, including LAT, SLP-76, phospholipase C-gamma2, but not Vav. Compared to wild-type Syk, Y342F Syk had decreased binding to phosphorylated immunoreceptor tyrosine-based activation motifs and reduced kinase activity. Surprisingly, mutation of Tyr346 had much less effect on Fc epsilon RI-dependent mast cell degranulation. An anti-Syk-phospho-346 tyrosine antibody indicated that antigen stimulation induced only a very minor increase in the phosphorylation of this tyrosine. Therefore, Tyr342, but not Tyr346, is critical for regulating Syk in mast cells and the function of these tyrosines in immune receptor signaling appears to be different from what has been previously reported for the equivalent residues of ZAP70.

Indexed as

Cell Cycle ProteinsAnimalsAntibodiesCalcimycinCalciumCell DegranulationCell LineEnzyme PrecursorsHumansImmunoglobulin EIntracellular Signaling Peptides and ProteinsIonophoresIsoenzymesMast CellsMitogen-Activated Protein KinasesMutagenesis, Site-DirectedAntibodiesCalcimycinCalciumCell Cycle ProteinsEnzyme PrecursorsImmunoglobulin EIntracellular Signaling Peptides and ProteinsIonophoresIsoenzymesMitogen-Activated Protein KinasesPeptidesPhospholipase C gammaProtein Kinase Cprotein kinase DProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-vavrac1 GTP-Binding ProteinReceptors, IgESyk KinaseSYK protein, humanSyk protein, ratType C PhospholipasesTyrosineVAV1 protein, humanVav1 protein, rat

Identifiers

PMID12417718
PMCPMC134060
OpenAlexW2119778247

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.