[doi: 10.5505/2017ichc.OP-30]Revealing Physical and Functional Interaction between p60-katanin and p53Şirin KoruluMicrotubules are dynamic polymers and that can be re-organized by assembly and disassembly phases, known as dynamic instability depending on the need of the cell. Besides, microtubule severing proteins such as katanin have roles in microtubule reconfiguration. Katanin is one of the most studied microtubule severing protein and is composed of two subunits, the catalytic subunit p60-katanin and p80-katanin. Microtubule severing mechanism of p60-katanin has been studied extensively for many years. However, interacting partners of p60-katanin are still very few. There are a few proteins identified so far that physically interact with p60-katanin. We have identified that p53 interacts with p60-katanin and this current study is specifically concentrated on the revealing of p53–p60-katanin structural interaction and the function of this interaction. To this aim, the cellular localization of the interaction was analyzed. Furthermore, deletion constructs were prepared for both p53 and p60-katanin. To reveal the interacting domains of the proteins, pull down assay was performed for the designed deletion constructs. Finally, to reveal the signaling pathways affected by p53–p60-katanin interaction, comparative genome wide transcriptome analysis was performed for the cells that p53–p60-katanin interaction is both ensured and disrupted. Since p53 is a critical protein between proliferation and differentiation, and p60-katanin has roles in both proliferation and differentiation, investigating effects of p53 on p60-katanin will shed light on not only the regulation of microtubule severing but also understanding the neurodegenerative diseases which indicate the correlations with reactivation of proliferation and degeneration of neurons and the molecular mechanism of p53-dependent changes of neurite retraction in neurodegeneration. |