K27-linked ubiquitylation promotes p97 substrate processing and is essential for cell proliferation

ABSTRACT: Conjugation of ubiquitin to numerous substrate proteins regulates virtually all cellular processes. Eight distinct ubiquitin polymer linkages specifying different functional outcomes are generated in cells. However, the roles of some atypical poly-ubiquitin topologies, in particular K27-linkages, remain poorly understood due to a lack of tools for their specific detection and manipulation. Here, we adapted a cell-based ubiquitin replacement strategy to enable specific and conditional abrogation of K27-linked ubiquitylation, revealing that this ubiquitin linkage type is essential for proliferation of human cells. We demonstrate that K27-linked ubiquitylation is predominantly a nuclear modification whose ablation deregulates nuclear ubiquitylation dynamics and impairs cell cycle progression

SUBMITTER: Dr. Robert, F Shearer 

PROVIDER: S-SCDT-10_15252-EMBJ_2021110145 | biostudies-other |

REPOSITORIES: biostudies-other