Hidemi Teramoto

TL;DR: It is shown that in COS-7 cells, activated Ras effectively stimulates MAPK but poorly induces JNK activity, which strongly support a critical role for Rac1 and Cdc42 in controlling the JNK signaling pathway.

TL;DR: It was necessary to fulfill all four conditions, i.e., integrin aggregation, integrin occupancy, tyrosine kinase activity, and actin cytoskeletal integrity, to achieve integrin- mediated focal accumulation of other cytoskeleton molecules including F- actin and paxillin.

TL;DR: It is shown that PGE2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein (G protein)–coupled receptor, EP2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase Akt and relieving the inhibitory phosphorylation of β-catenin and activating its signaling pathway.

TL;DR: These studies identify mechanisms in the signal transduction response to integrins and growth factors that require various combinations of integrin aggregation and ligands for integrin or growth factor receptors, providing opportunities for collaboration between these major regulatory systems.

TL;DR: It is found that MLK3 overexpression is sufficient to activate JNK potently without affecting the phosphorylating activity of MAPK or p38, and evidence is presented thatMLK3 binds the GTP-binding proteins Cdc42 and Rac1 in vivo and that MLk3 mediates activation of MEKK-SEK-JNK kinase cascade by Rac1 and CDC42.