IGF2BP1: a novel binding protein of p38 MAPK.

Signal transduction pathways control various biological processes in cells leading to distinct cellular functions. Protein-protein interactions and post-translational modifications are the physiological events that occur in signaling pathway. p38 MAPK are known to be involved in regulating wide range of cellular processes by interacting and activating relevant signaling molecules by means of phosphorylation. Deregulation of p38 MAPK is associated with various pathological conditions. In order to get an insight into the role played by p38 MAPK in cellular signaling, studies were carried out to identify proteins that interact with p38 MAPK. Mass spectrometry was used to identify the proteins present in p38 MAPK complex obtained by co-immunoprecipitation. Based on mass spectrometry data, here we report insulin-like growth factor-II binding protein 1 (IGF2BP1) as a novel interacting partner of p38 MAPK. IGF2BP1 is a RNA-binding protein predominantly known to be involved in tumor progression. To reconfirm the mass spectrometry data, in silico analysis was carried out. Based on different models predicted in silico, we report the possible interaction domains of p38MAPK and IGF2BP1. Considering the involvement of p38MAPK and IGF2BP1 in cancer, our study opens up the possibility of p38MAPK regulating IGF2BP1 function, and the possibility of targeting this novel interaction for developing cancer-treating drugs is discussed.