MNK2 Inhibits eIF4G Activation Through a Pathway Involving Serine-Arginine–Rich Protein Kinase in Skeletal Muscle

• DOI: 10.1126/scisignal.2002466
• Publication Date: 2012-02-14T21:26:03Z
• Authors: Shou-Ih Hu; Mark Katz; Sherry Chin; Xiaoqing Qi; Joseph Cruz; Chikwendu Ibebunjo; Shanchuan Zhao; Amy Chen; David J. Glass
• Keywords: Mice, Knockout; Sirolimus; 0301 basic medicine; Blotting, Western; Ribosomal Protein S6 Kinases, 70-kDa; Protein Serine-Threonine Kinases; Arginine; Dexamethasone; Cell Line; Myoblasts; Mice; Muscular Atrophy; 03 medical and health sciences; Serine; Animals; RNA Interference; Insulin-Like Growth Factor I; Phosphorylation; Eukaryotic Initiation Factor-4G; Muscle, Skeletal; Protein Binding; Signal Transduction

In muscle, the kinase-dependent and -independent functions of MNK2 inhibit the protein translation protein eIF4G under conditions that promote atrophy.