scholarly journals The protein-tyrosine kinase Syk interacts with TRAF-interacting protein TRIP in breast epithelial cells

Oncogene ◽  
2009 ◽  
Vol 28 (10) ◽  
pp. 1348-1356 ◽  
Author(s):  
Q Zhou ◽  
R L Geahlen
Keyword(s):  
Epithelial Cells ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Interacting Protein ◽  
Breast Epithelial Cells ◽  
Protein Tyrosine ◽  
Breast Epithelial

scholarly journals Induction of Protein Tyrosine Kinase 6 in Mouse Intestinal Crypt Epithelial Cells Promotes DNA Damage–Induced Apoptosis

2009 ◽  
Vol 137 (3) ◽  
pp. 945-954 ◽  
Author(s):  
Andrea Haegebarth ◽  
Ansu O. Perekatt ◽  
Wenjun Bie ◽  
Jessica J. Gierut ◽  
Angela L. Tyner
Keyword(s):  
Dna Damage ◽  
Epithelial Cells ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Intestinal Crypt ◽  
Protein Tyrosine ◽  
Induced Apoptosis

scholarly journals Protein Tyrosine Kinase 6 Negatively Regulates Growth and Promotes Enterocyte Differentiation in the Small Intestine

2006 ◽  
Vol 26 (13) ◽  
pp. 4949-4957 ◽  
Author(s):  
Andrea Haegebarth ◽  
Wenjun Bie ◽  
Ruyan Yang ◽  
Susan E. Crawford ◽  
Valeri Vasioukhin ◽  
...  
Keyword(s):  
Small Intestine ◽  
Epithelial Cells ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Cell Types ◽  
Intestinal Epithelial ◽  
Fatty Acid Binding ◽  
Protein Tyrosine ◽  
Adult Mice ◽  
Enterocyte Differentiation

ABSTRACT Protein tyrosine kinase 6 (PTK6) (also called Brk or Sik) is an intracellular tyrosine kinase that is expressed in breast cancer and normal epithelial linings. In adult mice, PTK6 expression is high in villus epithelial cells of the small intestine. To explore functions of PTK6, we disrupted the mouse Ptk6 gene. We detected longer villi, an expanded zone of PCNA expression, and increased bromodeoxyuridine incorporation in the PTK6-deficient small intestine. Although differentiation of major epithelial cell types occurred, there was a marked delay in expression of intestinal fatty acid binding protein, suggesting a role for PTK6 in enterocyte differentiation. However, fat absorption was comparable in wild-type and Ptk6 −/− mice. It was previously shown that the serine threonine kinase Akt is a substrate of PTK6 and that PTK6-mediated phosphorylation of Akt on tyrosine resulted in inhibition of Akt activity. Consistent with these findings, we detected increased Akt activity and nuclear β-catenin in intestines of PTK6-deficient mice and decreased nuclear localization of the Akt substrate FoxO1 in villus epithelial cells. PTK6 contributes to maintenance of tissue homeostasis through negative regulation of Akt in the small intestine and is associated with cell cycle exit and differentiation in normal intestinal epithelial cells.

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