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The binding of actin to p38 MAPK and inhibiting its kinase activity in vitro 被引量:2
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作者 杨琨 姜勇 +1 位作者 韩家淮 顾军 《Science China(Life Sciences)》 SCIE CAS 2003年第1期87-94,共8页
p38 MAP kinase mediates a signal pathway that is involved in many physiological and pathological processes such as inflammation, cellular stress, apoptosis, cell cycle and growth, ischemia/re-perfusion, and myocardium... p38 MAP kinase mediates a signal pathway that is involved in many physiological and pathological processes such as inflammation, cellular stress, apoptosis, cell cycle and growth, ischemia/re-perfusion, and myocardium hypertrophy. To determine the molecular and regulative mechanism of p38 signal pathway, we used in vitro binding methods to screen the proteins that interact with p38. Here we report two proteins from mouse macrophage RAW264.7 strain treated with lipopolysaccharide (LPS) or ultraviolet radiation (UV), binding directly to p38. One of them is b-actin identified by peptide mass spectrum and ProFound program. Actin can inhibit the auto-phosphorylation of p38 and the phosphorylation of ATF by p38. It suggests that the binding of actin to p38 in vitro may represent a negative feedback to the kinase activity of p38, which leads to the regulation of p38 pathway and cellular function. 展开更多
关键词 mitogen-activated protein kinase (map kinase mapk) p38 mapk actin protein-protein interaction signal transduction.
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