The binding of actin to p38 MAPK and inhibiting its kinase activity in vitro.
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 beta-actin identified by peptide mass spectrum and ProFound program. Actin can inhibit the autophosphorylation 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.
Yang
Kun
K
Research Center of Molecular Medicine, Sun Yet-sen University of Medical Sciences, Guangzhou 510080, China.
Jiang
Yong
Y
Han
Jiahuai
J
Gu
Jun
J
D000199:Actins / Q000378:metabolism*; D051698:Activating Transcription Factor 2 / Q000378:metabolism; D000818:Animals; D002460:Cell Line; D025461:Feedback, Physiological; D066298:In Vitro Techniques; D020935:MAP Kinase Signaling System; D051379:Mice; D010766:Phosphorylation; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D048051:p38 Mitogen-Activated Protein Kinases / Q000037:antagonists & inhibitors* / Q000378:metabolism*
D000199:Actins; D051698:Activating Transcription Factor 2; C497106:Atf2 protein, mouse; D011994:Recombinant Proteins; D048051:p38 Mitogen-Activated Protein Kinases