Direct stimulation of Bruton's tyrosine kinase by Gq-protein α-subunit

Bence, Kendra K.; Ma, Wei; Kozasa, Tohru; Huang, Xin‐Yun

doi:10.1038/38520

Cited by 184 publications

(154 citation statements)

References 28 publications

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“…This tantalizing link remains to be established. Similarly, the functional signi®cance of the ability of Ga q to stimulate the novel Bruton's tyrosine kinase remains to be established (Bence et al, 1997). Nevertheless it is interesting to note that the cells de®cient in BTK show a blunted p38MAPK-response to Ga q -coupled receptors (Bence et al, 1997).…”

Section: G Protein Interactions With Other Signaling Pathwaysmentioning

confidence: 99%

Regulation of cell proliferation by G proteins

Dhanasekaran

Tsim²,

Dermott³

et al. 1998

Oncogene

136

107

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G Proteins provide signal transduction mechanisms to seven transmembrane receptors. Recent studies have indicated that the a-subunits as well as the bg-subunits of these proteins regulate several critical signaling pathways involved in cell proliferation, di erentiation and apoptosis. Of the 17 a-subunits that have been cloned, at least ten of them have been shown to couple mitogenic signaling in ®broblast cells. Activating mutations in Ga s , Ga i2 , and Ga 12 have been correlated with di erent types of tumors. In addition, the ability of the bg-subunits to activate mitogenic pathways in di erent cell-types has been de®ned. The present review brie¯y summarizes the diverse and novel signaling pathways regulated by the a-as well as the bg-subunits of G proteins in regulating cell proliferation.

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Section: G Protein Interactions With Other Signaling Pathwaysmentioning

confidence: 99%

Regulation of cell proliferation by G proteins

Dhanasekaran

Tsim²,

Dermott³

et al. 1998

Oncogene

136

107

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“…Activation of p42/p44 MAPK by G i proteins is often associated with activation of the tyrosine-kinase Src, and it was proposed that Src was part of the molecular link between G i proteins and Shc (Chen et al, 1994;Luttrell et al, 1996). However, some authors assign GCRactivation of Src to G q , not G i , proteins (Wan et al, 1996;Kranenburg et al, 1997) and others suggest that other tyrosine-kinases (Btk, Itk, PYK-2, Syk) or phosphoinisotide 3' Kinase g (PI3Kg) link G i to Shc and the subsequent stimulation of the ERK-MAPK cascade and cell proliferation (Dikic et al, 1996;Wan et al, 1997;Bence et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Regulation by Gi2 proteins of v-fms-induced proliferation and transformation via Src-kinase and STAT3

1999

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We previously showed that G i2 proteins interfere with the transduction of CSF-1 receptor (CSF-1R) proliferation signals (Corre and Hermouet, 1995). To identify CSF-1R pathways controlled by G i2 , we transfected v-fms, the oncogenic equivalent of CSF-1R, in NIH3T3 cells in which G i2 proteins were inactivated by stably expressing a dominant negative mutant form of the a subunit of G i2 (a i2 -G204A). Expression of a i2 -G204A resulted in decreased Src-kinase activity, delayed activation of p42 ERK-MAPK, decreased cyclin D1 expression and reduced proliferation in response to serum. In a i2 -G204A cells transfected with v-fms, Src-kinase activity remained de®cient but p42 MAPK activity and cyclin D1 expression were similar to those of vector/v-fms cells, suggesting that v-fms bypasses Src to activate the ERK-MAPK cascade. However, DNA synthesis and focus formation were inhibited by up to 80% in a i2 -G204A/vfms cells compared to vector/v-fms cells. We found that tyrosine phosphorylation of STAT3, also activated by CSF-1R/v-fms, was inhibited in a i2 -G204A/v-fms cells; in addition, expression of an 85 kDa, C-terminal truncated form of STAT3 (STAT3D) was constitutively increased. Both the inhibition of v-fms-induced STAT3 tyrosine phosphorylation and the increased expression of STAT3D were reproduced by transfecting a dominant negative mutant of Src. Last, we show that expression of STAT3D55C, a mutant form of STAT3 lacking the last 55 C-terminal amino acids, is su cient to inhibit DNA synthesis and v-fms-induced transformation in NIH3T3 cells. In summary, adequate regulation by G i2 proteins of the activity of both Src-kinase and STAT3 is required for optimal cell proliferation in response to CSF-1R/vfms.

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“…The PH-TH domain of Btk has been shown to bind to bg, Gaq and Ga12 subunit of heterotrimeric G-proteins (LanghansRajasekaran et al, 1995;Bence et al, 1997;Touhara et al, 1994;Tsukada et al, 1994) and the association results in elevation of kinase activity (Jiang et al, 1998;Langhans-Rajasekaran et al, 1995;Ma and Huang, 1998). In addition, Tec and Bmx/Etk are also regulated by Ga12/13.…”

Section: Interaction With Heterotrimeric G-protein Subunitsmentioning

confidence: 99%

Signaling network of the Btk family kinases

Qiu¹,

2000

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The Btk family kinases represent new members of nonreceptor tyrosine kinases, which include Btk/Atk, Itk/ Emt/Tsk, Bmx/Etk, and Tec. They are characterized by having four structural modules: PH (pleckstrin homology) domain, SH3 (Src homology 3) domain, SH2 (Src homology 2) domain and kinase (Src homology 1) domain. Increasing evidence suggests that, like Srcfamily kinases, Btk family kinases play central but diverse modulatory roles in various cellular processes. They participate in signal transduction in response to virtually all types of extracellular stimuli which are transmitted by growth factor receptors, cytokine receptors, G-protein coupled receptors, antigen-receptors and integrins. They are regulated by many non-receptor tyrosine kinases such as Src, Jak, Syk and FAK family kinases. In turn, they regulate many of major signaling pathways including those of PI3K, PLCg and PKC. Both genetic and biochemical approaches have been used to dissect the signaling pathways and elucidate their roles in growth, di erentiation and apoptosis. An emerging new role of this family of kinases is cytoskeletal reorganization and cell motility. The physiological importance of these kinases was amply demonstrated by their link to the development of immunode®ciency diseases, due to germ-line mutations. The present article attempts to review the structure and functions of Btk family kinases by summarizing our current knowledge on the interacting partners associated with the di erent modules of the kinases and the diverse signaling pathways in which they are involved. Oncogene (2000) 19, 5651 ± 5661.

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Direct stimulation of Bruton's tyrosine kinase by Gq-protein α-subunit

Cited by 184 publications

References 28 publications

Regulation of cell proliferation by G proteins

Regulation of cell proliferation by G proteins

Regulation by Gi2 proteins of v-fms-induced proliferation and transformation via Src-kinase and STAT3

Signaling network of the Btk family kinases

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