Activation of Tsk and Btk tyrosine kinases by G protein βγ subunits

Sigrid A. Langhans-Rajasekaran, Yong Wan, Xin Yun Huang*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

124 Scopus citations

Abstract

Tsk/Itk and Btk are members of the pleckstrin-homology (PH) domain- containing tyrosine kinase family. The PH domain has been demonstrated to be able to interact with βγ subunits of heterotrimeric guanine nucleotide- binding proteins (G proteins) (G(βγ)) and phospholipids. Using cotransfection assays, we show here that the kinase activities of Tsk and Btk are stimulated by certain G(βγ), subunits. Furthermore, using an in vitro reconstitution assay with purified bovine brain G(βγ) subunits and the immunoprecipitated Tsk, we find that Tsk kinase activity is increased by G(βγ) subunits and another membrane factor(s). These results indicate that this family of tyrosine kinases could be an effector of heterotrimeric G proteins.

Original languageEnglish (US)
Pages (from-to)8601-8605
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number19
DOIs
StatePublished - Sep 12 1995

Keywords

  • pleckstrin-homology domain
  • signal transduction

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Activation of Tsk and Btk tyrosine kinases by G protein βγ subunits'. Together they form a unique fingerprint.

Cite this