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

Sigrid A. Langhans-Rajasekaran; Yong Wan; Xin Yun Huang

doi:10.1073/pnas.92.19.8601

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

Obstetrics and Gynecology

Research output: Contribution to journal › Article › peer-review

127 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 language	English (US)
Pages (from-to)	8601-8605
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	92
Issue number	19
DOIs	https://doi.org/10.1073/pnas.92.19.8601
State	Published - Sep 12 1995

Keywords

pleckstrin-homology domain
signal transduction

ASJC Scopus subject areas

General

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10.1073/pnas.92.19.8601

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title = "Activation of Tsk and Btk tyrosine kinases by G protein βγ subunits",

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.",

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T1 - Activation of Tsk and Btk tyrosine kinases by G protein βγ subunits

AU - Langhans-Rajasekaran, Sigrid A.

AU - Wan, Yong

AU - Huang, Xin Yun

PY - 1995/9/12

Y1 - 1995/9/12

N2 - 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.

AB - 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.

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

Abstract

Keywords

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