Gopal Sapkota has published a single-author research paper in Open BIology that puts a question mark on the notion that transforming growth factor beta (TGFÃ_Â_) activates TGFÃ_Â_ Activated Kinase 1 (TAK1).
The activation of p38 MAPK by transforming growth factor Ã_Â_ (TGFÃ_Â_) plays an important role in determining cell fate. It was long thought that a protein kinase termed TAK1 (TGFÃ_Â_ activated kinase 1; also known as MAP3K7) was responsible for the TGFÃ_Â_-induced activation of p38 MAPK in cells. By employing mouse embryo fibroblasts derived from TAK1-deficient mice, Gopal's research demonstrates that TAK1 is dispensable for TGFÃ_Â_-induced activation of p38 MAPK. Instead his research proposes the role for two other protein kinases, namely MAP3K4 andMAP3K10, in mediating the activation of p38 MAPK in response to TGFÃ_Â_.
To read Gopal's paper entitled 'The TGFÃ_Â_-induced phosphorylation and activation of p38 mitogen-activated protein kinase is mediated by MAP3K4 and MAP3K10 but not TAK1' please click here
The activation of p38 MAPK by transforming growth factor Ã_Â_ (TGFÃ_Â_) plays an important role in determining cell fate. It was long thought that a protein kinase termed TAK1 (TGFÃ_Â_ activated kinase 1; also known as MAP3K7) was responsible for the TGFÃ_Â_-induced activation of p38 MAPK in cells. By employing mouse embryo fibroblasts derived from TAK1-deficient mice, Gopal's research demonstrates that TAK1 is dispensable for TGFÃ_Â_-induced activation of p38 MAPK. Instead his research proposes the role for two other protein kinases, namely MAP3K4 andMAP3K10, in mediating the activation of p38 MAPK in response to TGFÃ_Â_.
To read Gopal's paper entitled 'The TGFÃ_Â_-induced phosphorylation and activation of p38 mitogen-activated protein kinase is mediated by MAP3K4 and MAP3K10 but not TAK1' please click here