Evidence map›Paper›PMID 16611990›Full record

ArticleMolecular and cellular biology2006

Nucleocytoplasmic trafficking of the Syk protein tyrosine kinase.

Fei Zhou, Jianjie Hu, Haiyan Ma, Marietta L Harrison, Robert L Geahlen

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.7field-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

36 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Expression of Syk and MAP4 proteins in ovarian cancer.Journal of cancer research and clinical oncology · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Quantitative immunofluorescence reveals the signature of active B-cell receptor signaling in diffuse large B-cell lymphoma.Clinical cancer research : an official journal of the American Association for Cancer Research · 2012
    Article
  19. Article
  20. Serine phosphorylation by SYK is critical for nuclear localization and transcription factor function of Ikaros.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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.

Fei ZhouDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 201 S. University St., West Lafayette, IN 47907-2064, USA.
Jianjie Hu
Haiyan Ma
Marietta L Harrison
Robert L Geahlen
Purdue University West Lafayette · US

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
TYROSINE PROTEIN KINASES AND LYMPHOCYTE ACTIVATIONR01CA037372 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI GEAHLEN, ROBERT L · 1985 to 2011
$3.5M
NCI NIH HHS CA37372NCI NIH HHS P30 CA023168NCI NIH HHS P30 CA23168NCI NIH HHS R01 CA037372
6 · The paper itself

Abstract

The protein tyrosine kinase Syk couples the B-cell receptor (BCR) for antigen to multiple intracellular signaling pathways and also modulates cellular responses to inducers of oxidative stress in a receptor-independent fashion. In B cells, Syk is found in both the nuclear and cytoplasmic compartments but contains no recognizable nuclear localization or export signals. Through the analysis of a series of deletion mutants, we identified the presence of an unconventional shuttling sequence near the junction of the catalytic domain and the linker B region that accounts for Syk's subcellular localization. This localization is altered following prolonged engagement of the BCR, which causes Syk to be excluded from the nucleus. Nuclear exclusion requires the receptor-mediated activation of protein kinase C and new protein synthesis. Both of these processes also potentiate the activation of caspase 3 in cells in response to oxidative stress in a manner that is dependent on the localization of Syk outside of the nucleus. In contrast, restriction of Syk to the nucleus greatly diminishes the stress-induced activation of caspase 3.

Indexed as

AnimalsAntibodies, Anti-IdiotypicB-LymphocytesCaspase 3CaspasesCatalytic DomainCell NucleusCells, CulturedCytoplasmDNA Mutational AnalysisEnzyme ActivationGreen Fluorescent ProteinsImmunoglobulin MIntracellular Signaling Peptides and ProteinsNuclear Localization SignalsProtein BiosynthesisAntibodies, Anti-IdiotypicCaspase 3CaspasesGreen Fluorescent ProteinsImmunoglobulin MIntracellular Signaling Peptides and ProteinsNuclear Localization SignalsProtein Kinase CProtein-Tyrosine KinasesSyk KinaseTetradecanoylphorbol Acetate

Identifiers

PMID16611990
PMCPMC1447433
OpenAlexW2137210893

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.