Dissecting the role of CRLcdt2 in the maintenance of chromatin stability

EZEQUIEL CALVO-ROITBERG; JULIANA ENRIQUÉ STEINBERG; JOAQUIN M ESPINOSA; FABIANA ALEJANDRA ROSSI; MARIO ROSSI

Bariloche

Simposio; Fourth South American Spring Symposium in Signal Transduction and Molecular Medicine (SISTAM); 2018

The formation and progression of cancer is ultimately regulated by the abundance and activity of both oncogenic and tumor suppressor proteins. The Ubiquitin-Proteasome System consists of a complex network of enzymes where the E3 ligases are the final effectors and dictate the specificity of the UPS machinery. CRL4Cdt2 ubiquitin ligase is emerging as a master regulator of cellular proliferation involved in multiple DNA repair processes. In order to broaden our understanding how deregulation of CRL4Cdt2 might contribute to cancer development, we used an affinity purification and mass spectrometry approach to identify and characterize novel CRL4Cdt2 substrates. Among the most abundant putative Cdt2 protein interacting factors identified, we center our work on different members of a multi-protein complex implicated in the maintenance of chromatin structure, gene transcription and DNA replication