p38 is a kinase protein belonging to a family of MAPK responsible for relaying extracellular signals into cellular response, and plays a central role in plethora of cellular signaling events. p38 predominantly gets activated via trans-phosphorylation involving 3 tiers of kinases also knows as the classical MAPKKK cascade, however, it can also get activated via autophosphorylation in cis, induced by a scaffolding protein known as TAB1. The latter form of p38α activation induced by TAB1 has been associated with the pernicious effect seen in myocardial infarction. In fact, preventing the interaction between p38α and TAB1 attenuates the damage to the heart. As p38α activation via TAB1 seems to be specific to myocardial infarction, we could exploit this phenomenon as a better therapeutic approach to ischemic cardiovascular disease which avoids the toxicity problem seen in clinical trials with p38 inhibitors. The aim of this project is to study the interaction between p38α and TAB1, in order to target it and discover novel tools to disrupt this signaling event. I have used cell culture, western blot, pcr/cloning, protein purification and IVK assays for my project and shown that TAB1 causes p38 autophosphorylation and discovered important structural residues that may play important role in this process.
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