作者: Kazumasa Ohashi , Kyoko Nagata , Midori Maekawa , Toshimasa Ishizaki , Shuh Narumiya
关键词: Phosphorylation 、 MAP2K7 、 Protein phosphorylation 、 Serine/threonine-specific protein kinase 、 Protein kinase A 、 Chemistry 、 Cell biology 、 Molecular biology 、 PAK1 、 Lim kinase 、 Kinase activity 、 Biochemistry
摘要: LIM-kinase 1 (LIMK1) phosphorylates cofilin, an actin-depolymerizing factor, and regulates actin cytoskeletal reorganization. LIMK1 is activated by the small GTPase Rho its downstream protein kinase ROCK. We now report site of phosphorylation In vitro reaction revealed that active forms ROCK phosphorylated on threonine residue markedly increased cofilin-phosphorylating activity. A mutant (T508A) with replacement Thr-508 within activation loop domain alanine was neither nor Replacement serine changed ROCK-catalyzed from to serine. two glutamates activity about 2-fold but not further addition, wild-type LIMK1, T508A mutant, co-expression in cultured cells. These results suggest activates vivo at Thr-508. Together recent finding PAK1, a effector Rac, also Thr-508, these one common targets for Rac reorganize cytoskeleton.