Evidence map›Paper›PMID 7518558›Full record

ArticleMolecular and cellular biology1994

Tyrosine phosphorylation and activation of Bruton tyrosine kinase upon Fc epsilon RI cross-linking.

Y Kawakami, L Yao, T Miura, S Tsukada, O N Witte, T Kawakami

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

66 citing papers in PubMed, 218 citations in OpenAlex.

  1. Trial
  2. Two-step mechanism of Bruton's tyrosine kinase membrane recruitment and activation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Autoallergy and what the Allergist Needs to know.Current allergy and asthma reports · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Bruton's Tyrosine Kinase and Its Isoforms in Cancer.Frontiers in cell and developmental biology · 2021
    Review
  15. Kinase inhibition in autoimmunity and inflammation.Nature reviews. Drug discovery · 2021
    Review
  16. Review
  17. Structural mechanism for Bruton's tyrosine kinase activation at the cell membrane.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Review
  19. Article
  20. From IgE to Omalizumab.Journal of immunology (Baltimore, Md. : 1950) · 2016
    Review

6 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Y KawakamiDivision of Immunobiology, La Jolla Institute for Allergy and Immunology, California 92037.
L Yao
T Miura
S Tsukada
O N Witte
T Kawakami
La Jolla Institute for Immunology · US

Funding

NIAID NIH HHS AI-10060
6 · The paper itself

Abstract

Tyrosine phosphorylation of several cellular proteins is one of the earliest signaling events induced by cross-linking of the high-affinity receptor for immunoglobulin E (Fc epsilon RI) on mast cells or basophils. Tyrosine kinases activated during this process include the Src family kinases, Lyn, c-Yes, and c-Src, and members of another subfamily, Syk and PTK72 (identical or highly related to Syk). Recently, some of us described two novel tyrosine kinases, Emb and Emt, whose expression was limited to subsets of hematopoietic cells, including mast cells. Emb turned out to be identical to Btk, a gene product defective in human X-linked agammaglobulinemia and in X-linked immunodeficient (xid) mice. Here we report that Fc epsilon RI cross-linking induced rapid phosphorylation on tyrosine, serine, and threonine residues and activation of Btk in mouse bone marrow-derived mast cells. A small fraction of Btk translocated from the cytosol to the membrane compartment following receptor cross-linking. Tyrosine phosphorylation of Btk was not induced by either a Ca2+ ionophore (A23187), phorbol 12-myristate 13-acetate, or a combination of the two reagents. Co-immunoprecipitation between Btk and receptor subunit beta or gamma was not detected. The data collectively suggest that Btk is not associated with Fc epsilon but that its activation takes place prior to protein kinase C activation and plays a novel role in the Fc epsilon RI signaling pathway.

Indexed as

Signal Transductionsrc-Family KinasesAgammaglobulinaemia Tyrosine KinaseAnimalsCell CompartmentationEnzyme ActivationIn Vitro TechniquesMast CellsMiceMitogensPhosphotyrosineProtein-Tyrosine KinasesReceptor AggregationReceptors, IgETyrosineAgammaglobulinaemia Tyrosine KinaseBTK protein, humanBtk protein, mouselyn protein-tyrosine kinaseMitogensPhosphotyrosineProtein-Tyrosine KinasesReceptors, IgEsrc-Family KinasesTyrosine

Identifiers

PMID7518558
PMCPMC359029
OpenAlexW1945380293

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.