The protein kinase DYRK2 as a new regulator of protein homeostasis

Wednesday 12th August 2020

12:00 - 13:00hrs via zoom

 

Cancer cells are exposed to high levels of cellular stress and they depend on stress-relief pathways in order to survive and proliferate. To survive the proteotoxic stress produced by the accumulation of excess and often misfolded proteins, cancer cells can either a) increase protein folding capacity (controlled by the transcription factor HSF1 ) or b) increase protein degradation (by the autophagy and ubiquitin proteasome system). In this talk I will show how in triple negative breast cancer (TNBC) cells, the dual-specificity tyrosine-regulated kinase 2 (DYRK2) is an upstream positive regulator of both HSF1 and the proteasome. This presents DYRK2 as a positive regulator of two main mechanisms by which aneuploid cells adapt, survive and become malignant, and thus highlights this kinase as a potential therapeutic target.

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