Ethanol-Induced Cas Tyrosine Phosphorylation and Fyn Kinase Activation in Rat Brain

2002 ◽  
Vol 26 (Supplement) ◽  
pp. 38S-43S
Author(s):  
Hajime Nishio ◽  
Koichi Suzuki
Keyword(s):  
Rat Brain ◽  
Tyrosine Phosphorylation ◽  
Kinase Activation ◽  
Fyn Kinase

scholarly journals Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell–cell adhesion

2002 ◽  
Vol 156 (1) ◽  
pp. 137-148 ◽  
Author(s):  
Enzo Calautti ◽  
Maddalena Grossi ◽  
Cristina Mammucari ◽  
Yumi Aoyama ◽  
Maria Pirro ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Kinase Activation ◽  
Positive Effects ◽  
Fyn Kinase ◽  
Keratinocyte Cell ◽  
Downstream Mediator ◽  
Cell Cell ◽  
Fyn Tyrosine Kinase

The Rho GTPase and Fyn tyrosine kinase have been implicated previously in positive control of keratinocyte cell–cell adhesion. Here, we show that Rho and Fyn operate along the same signaling pathway. Endogenous Rho activity increases in differentiating keratinocytes and is required for both Fyn kinase activation and increased tyrosine phosphorylation of β- and γ-catenin, which is associated with the establishment of keratinocyte cell–cell adhesion. Conversely, expression of constitutive active Rho is sufficient to promote cell–cell adhesion through a tyrosine kinase- and Fyn-dependent mechanism, trigger Fyn kinase activation, and induce tyrosine phosphorylation of β- and γ-catenin and p120ctn. The positive effects of activated Rho on cell–cell adhesion are not induced by an activated Rho mutant with defective binding to the serine/threonine PRK2/PKN kinases. Endogenous PRK2 kinase activity increases with keratinocyte differentiation, and, like activated Rho, increased PRK2 activity promotes keratinocyte cell–cell adhesion and induces tyrosine phosphorylation of β- and γ-catenin and Fyn kinase activation. Thus, these findings reveal a novel role of Fyn as a downstream mediator of Rho in control of keratinocyte cell–cell adhesion and implicate the PRK2 kinase, a direct Rho effector, as a link between Rho and Fyn activation.

scholarly journals Selective activation of p42 mitogen-activated protein (MAP) kinase in murine B lymphoma cell lines by membrane immunoglobulin cross-linking. Evidence for protein kinase C-independent and -dependent mechanisms of activation

1992 ◽  
Vol 287 (1) ◽  
pp. 269-276 ◽  
Author(s):  
M R Gold ◽  
J S Sanghera ◽  
J Stewart ◽  
S L Pelech
Keyword(s):  
Map Kinase ◽  
Tyrosine Phosphorylation ◽  
Cell Lines ◽  
Map Kinases ◽  
Phorbol Esters ◽  
Cross Linking ◽  
Kinase Activation ◽  
Membrane Immunoglobulin ◽  
Protein Map ◽  
Mitogen Activated Protein

Cross-linking of membrane immunoglobulin (mIg), the B lymphocyte antigen receptor, with anti-receptor antibodies stimulates tyrosine phosphorylation of a number of proteins, including one of 42 kDa. Proteins with a similar molecular mass are tyrosine-phosphorylated in response to receptor stimulation in other cell types and have been identified as serine/threonine kinases, termed mitogen-activated protein (MAP) kinases or extracellular signal-regulated kinases (ERKs). The MAP kinases constitute a family of related kinases, at least three of which have molecular masses of 40-45 kDa. In this paper we show that mIg cross-linking stimulated the myelin basic protein phosphotransferase activity characteristic of MAP kinase in both mature and immature murine B cell lines. This enzyme activity co-purified on three different columns with a 42 kDa protein that was tyrosine-phosphorylated (pp42) in response to mIg cross-linking and which reacted with a panel of anti-(MAP kinase) antibodies. Although immunoblotting with the anti-(MAP kinase) antibodies showed that these B cell lines expressed both 42 kDa and 44 kDa forms of MAP kinase, only the 42 kDa form was activated and tyrosine-phosphorylated to a significant extent. Activation of protein kinase C (PKC) with phorbol esters also resulted in selective tyrosine phosphorylation and activation of the 42 kDa MAP kinase. This suggested that mIg-induced MAP kinase activation could be due to stimulation of PKC by mIg. However, mIg-stimulated MAP kinase activation and pp42 tyrosine phosphorylation was only partially blocked by a PKC inhibitor, the staurosporine analogue Compound 3. In contrast, Compound 3 completely blocked the ability of phorbol esters to stimulate MAP kinase activity and induce tyrosine phosphorylation of pp42. Thus mIg may activate MAP kinase by both PKC-dependent and -independent mechanisms.

scholarly journals Fyn kinase contributes to tyrosine phosphorylation of the GABAA receptor γ2 subunit

2010 ◽  
Vol 44 (2) ◽  
pp. 129-134 ◽  
Author(s):  
Rachel Jurd ◽  
Verena Tretter ◽  
Joshua Walker ◽  
Nicholas J. Brandon ◽  
Stephen J. Moss
Keyword(s):  
Tyrosine Phosphorylation ◽  
Gabaa Receptor ◽  
Fyn Kinase

scholarly journals Phosphorylation of p27Kip1 Regulates Assembly and Activation of Cyclin D1-Cdk4

2008 ◽  
Vol 28 (20) ◽  
pp. 6462-6472 ◽  
Author(s):  
Michelle D. Larrea ◽  
Jiyong Liang ◽  
Thiago Da Silva ◽  
Feng Hong ◽  
Shan H. Shao ◽  
...  
Keyword(s):  
Complex Formation ◽  
Cyclin D1 ◽  
Tyrosine Phosphorylation ◽  
Combined Therapy ◽  
Src Family Kinases ◽  
Kinase Activation ◽  
Constitutive Activation ◽  
Catalytic Activation ◽  
Inhibitory Function

ABSTRACT p27 mediates Cdk2 inhibition and is also found in cyclin D1-Cdk4 complexes. The present data support a role for p27 in the assembly of D-type cyclin-Cdk complexes and indicate that both cyclin D1-Cdk4-p27 assembly and kinase activation are regulated by p27 phosphorylation. Prior work showed that p27 can be phosphorylated by protein kinase B/Akt (PKB/Akt) at T157 and T198. Here we show that PKB activation and the appearance of p27pT157 and p27pT198 precede p27-cyclin D1-Cdk4 assembly in early G1. PI3K/PKB inhibition rapidly reduced p27pT157 and p27pT198 and dissociated cellular p27-cyclin D1-Cdk4. Mutant p27 allele products lacking phosphorylation at T157 and T198 bound poorly to cellular cyclin D1 and Cdk4. Cellular p27pT157 and p27pT198 coprecipitated with Cdk4 but were not detected in Cdk2 complexes. The addition of p27 to recombinant cyclin D1 and Cdk4 led to cyclin D1-Cdk4-p27 complex formation in vitro. p27 phosphorylation by PKB increased p27-cyclin D1-Cdk4 assembly in vitro but yielded inactive Cdk4. In contrast, Src pretreatment of p27 did not affect p27-cyclin D1-Cdk4 complex formation. However, Src treatment led to tyrosine phosphorylation of p27 and catalytic activation of assembled cyclin D1-Cdk4-p27 complexes. Thus, while PKB-dependent p27 phosphorylation appears to increase cyclin D1-Cdk4-p27 assembly or stabilize these complexes in vitro, cyclin D1-Cdk4-p27 activation requires the tyrosine phosphorylation of p27. Constitutive activation of PKB and Abl or Src family kinases in cancers would drive p27 phosphorylation, increase cyclin D1-Cdk4 assembly and activation, and reduce the cyclin E-Cdk2 inhibitory function of p27. Combined therapy with both Src and PI3K/PKB inhibitors may reverse this process.

scholarly journals Compartmentation of Fyn Kinase with Glycosylphosphatidylinositol-anchored Molecules in Oligodendrocytes Facilitates Kinase Activation during Myelination

1999 ◽  
Vol 274 (41) ◽  
pp. 29042-29049 ◽  
Author(s):  
Eva-Maria Krämer ◽  
Corinna Klein ◽  
Thomas Koch ◽  
Monica Boytinck ◽  
Jacqueline Trotter
Keyword(s):  
Kinase Activation ◽  
Fyn Kinase
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