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Article

Phosphatidylinositol 3-kinase-gamma activates Bruton's tyrosine kinase in concert with Src family kinases.

Proceedings of the National Academy of Sciences of the United States of America - 9 Dec 1997

Li Z, Wahl M I, Eguinoa A, Stephens L R, Hawkins P T, Witte O N

Abstract excerpt

Bruton's tyrosine kinase (Btk) is essential for normal B lymphocyte development and function. The activity of Btk is partially regulated by transphosphorylation within its kinase domain by Src family kinases at residue Tyr-551 and subsequent autophosphorylation at Tyr-223. Activation correlates with Btk association with cellular membranes. Based on specific loss of function mutations, the Btk pleckstrin homology...

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Identifiers

PMID: 9391111
DOI: 10.1073/pnas.94.25.13820
PMCID: PMC28391

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Phosphatidylinositol 3-kinase-gamma activates Bruton's tyrosine kinase in concert with Src family kinases.PMID 9391111Read ↗

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An SH3-binding site conserved in Bruton's tyrosine kinase and related tyrosine kinases mediates specific protein interactions in vitro and in vivo.Semantic proximity Read ↗

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