The binding of actin to p38 MAPK and inhibiting its kinase activity<Emphasis Type="Italic">in vitro</Emphasis> |
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Authors: | Kun?Yang Yong?Jiang Jiahuai?Han Email author" target="_blank">Jun?GuEmail author |
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Institution: | 1.Research Center of Molecular Medicine,Sun Yet-sen University of Medical Sciences,Guangzhou,China;2.Department of Pathophysiology and Key Laboratory for Shock and Microcirculation of PLA,The First Military Medical University,Guangzhou,China;3.Department of Immunology,The Scripps Research Institute,California,USA;4.Laboratory of Genetics, College of Life Science,Peking University,Beijing,China |
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Abstract: | 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 usedin 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 β-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 p38in vitro may represent a negative feedback to the kinase activity of p38, which leads to the regulation of p38 pathway and cellular
function. |
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Keywords: | mitogen-activated protein kinase (MAP kinase MAPK) p38 MAPK actin protein-protein interaction signal transduction |
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