Control of neuronal pathway selection by a Drosophila receptor protein-tyrosine kinase family member

Nature ◽  
1995 ◽  
Vol 376 (6536) ◽  
pp. 171-174 ◽  
Author(s):  
Christopher A. Callahan ◽  
M. G. Muralidhar ◽  
Scott E. Lundgren ◽  
Audra L. Scully ◽  
John B. Thomas
Keyword(s):  
Tyrosine Kinase ◽  
Family Member ◽  
Protein Tyrosine Kinase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Kinase Family ◽  
Neuronal Pathway ◽  
Receptor Protein Tyrosine Kinase

scholarly journals Characterization of B61, the Ligand for the Eck Receptor Protein-Tyrosine Kinase

1995 ◽  
Vol 270 (10) ◽  
pp. 5636-5641 ◽  
Author(s):  
Haining Shao ◽  
Akhilesh Pandey ◽  
K. Sue O'Shea ◽  
Michael Seldin ◽  
Vishva M. Dixit
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Kinase

scholarly journals Biochemical characterization of the protein tyrosine kinase homology domain of the ErbB3 (HER3) receptor protein

1997 ◽  
Vol 322 (3) ◽  
pp. 757-763 ◽  
Author(s):  
Susan L. SIERKE ◽  
Kunrong CHENG ◽  
Hong-Hee KIM ◽  
John G. KOLAND
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Egf Receptor ◽  
Biochemical Characterization ◽  
Cd Spectroscopy ◽  
Receptor Protein ◽  
Tyrosine Kinase Domain ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Kinase ◽  
Her3 Receptor

The putative protein tyrosine kinase domain (TKD) of the ErbB3 (HER3) receptor protein was generated as a histidine-tagged recombinant protein (hisTKD-B3) and characterized enzymologically. CD spectroscopy indicated that the hisTKD-B3 protein assumed a native conformation with a secondary structure similar to that of the epidermal growth factor (EGF) receptor TKD. However, when compared with the EGF receptor-derived protein, hisTKD-B3 exhibited negligible intrinsic protein tyrosine kinase activity. Immune complex kinase assays of full-length ErbB3 proteins also yielded no evidence of catalytic activity. A fluorescence assay previously used to characterize the nucleotide-binding properties of the EGF receptor indicated that the ErbB3 protein was unable to bind nucleotide. The hisTKD-B3 protein was subsequently found to be an excellent substrate for the EGF receptor protein tyrosine kinase, which suggested that in vivophosphorylation of ErbB3 in response to EGF could be attributed to a direct cross-phosphorylation by the EGF receptor protein tyrosine kinase.

scholarly journals Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk.

1995 ◽  
Vol 92 (6) ◽  
pp. 1866-1870 ◽  
Author(s):  
B. D. Bennett ◽  
F. C. Zeigler ◽  
Q. Gu ◽  
B. Fendly ◽  
A. D. Goddard ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Molecular Cloning ◽  
Protein Tyrosine Kinase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Kinase

scholarly journals Hepatitis C virus NS5A protein interacts with and negatively regulates the non-receptor protein tyrosine kinase Syk

2008 ◽  
Vol 89 (5) ◽  
pp. 1231-1242 ◽  
Author(s):  
Sachiko Inubushi ◽  
Motoko Nagano-Fujii ◽  
Kikumi Kitayama ◽  
Motofumi Tanaka ◽  
Chunying An ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Kinase Assay ◽  
Receptor Protein ◽  
Hcv Rna ◽  
Physical Interaction ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Kinase

Hepatitis C virus (HCV) is the major causative agent of hepatocellular carcinoma. However, the precise mechanism underlying the carcinogenesis is yet to be elucidated. It has recently been reported that Syk, a non-receptor protein tyrosine kinase, functions as a potent tumour suppressor in human breast carcinoma. This study first examined the possible effect of HCV infection on expression of Syk in vivo. Immunohistochemical analysis revealed that endogenous Syk, which otherwise was expressed diffusely in the cytoplasm of normal hepatocytes, was localized near the cell membrane with a patchy pattern in HCV-infected hepatocytes. The possible interaction between HCV proteins and Syk in human hepatoma-derived Huh-7 cells was then examined. Immunoprecipitation analysis revealed that NS5A interacted strongly with Syk. Deletion-mutation analysis revealed that an N-terminal portion of NS5A (aa 1–175) was involved in the physical interaction with Syk. An in vitro kinase assay demonstrated that NS5A inhibited the enzymic activity of Syk and that, in addition to the N-terminal 175 residues, a central portion of NS5A (aa 237–302) was required for inhibition of Syk. Moreover, Syk-mediated phosphorylation of phospholipase C-γ1 was downregulated by NS5A. An interaction of NS5A with Syk was also detected in Huh-7.5 cells harbouring an HCV RNA replicon or infected with HCV. In conclusion, these results demonstrated that NS5A interacts with Syk resulting in negative regulation of its kinase activity. The results indicate that NS5A may be involved in the carcinogenesis of hepatocytes through the suppression of Syk kinase activities.

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