Our group studies regulation of the cell cycle, focusing on processes required to rebuild interphase cells after mitosis. For example each daughter cell must adhere to its surroundings, assemble a nucleus around the chromatids it has inherited, and re-build networks of organelles (mitochondria, Golgi etc) that fragmented during mitosis. Ubiquitin-mediated proteolysis, orchestrated by the ubiquitin ligase known as Anaphase Promoting Complex (APC/C), controls many events at this time in the cell cycle. APC/C typically targets substrates for rapid degradation at mitotic exit and through G1 phase. Recently we have adopted a systems approach to describe the mitotic exit ‘ubiquitome’, a high confidence dataset of proteins that undergo ubiquitination specifically during this transition in the cell cycle. Some of the top hits in our ubiquitome dataset are proteins not previously known to undergo specific ubiquitination during mitotic exit, including the nuclear lamins (Lamin A, Lamin B1, Lamin B2) that assemble in networks under the nuclear envelope and influence chromatin organization within the nucleus. Our preliminary findings suggest that ubiquitination of these substrates does not signal their degradation, but correlates with highly specific patterns of localization in G1 phase. We are offering a PhD project that will use a combination of live cell imaging and biochemical approaches to unravel the different steps in assembly of lamin networks during transition from mitosis to interphase. The project will aim to identify pathways controlling ubiquitination of lamins during mitotic exit and to establish the fate of the ubiquitinated proteins and their contribution to establishing interphase.