EDD, a Ubiquitin-protein Ligase of the N-end Rule Pathway, Associates with Spindle Assembly Checkpoint Components and Regulates the Mitotic Response to Nocodazole
Copyright policy )EDD, a Ubiquitin-protein Ligase of the N-end Rule Pathway, Associates with Spindle Assembly Checkpoint Components and Regulates the Mitotic Response to Nocodazole
In this work, we identify physical and genetic interactions that implicate E3 identified by differential display (EDD) in promoting spindle assembly checkpoint (SAC) function. During mitosis, the SAC initiates a mitotic checkpoint in response to chromosomes with kinetochores unattached to spindle pole microtubules. Similar to Budding uninhibited by benzimidazoles-related 1 (BUBR1) siRNA, a bona fide SAC component, EDD siRNA abrogated G2/M accumulation in response to the mitotic destabilizing agent nocodazole. Furthermore, EDD siRNA reduced mitotic cell viability and, in nocodazole-treated cells, increased expression of the promitotic progression protein cell division cycle 20 (CDC20). Copurification studies also identified physical interactions with CDC20, BUBR1, and other components of the SAC. Taken together, these observations highlight the potential role of EDD in regulating mitotic progression and the cellular response to perturbed mitosis.
- University of Edinburgh United Kingdom
- Institute of Genetics and Cancer United Kingdom
- Universtity of Edinburgh United Kingdom
- Medical Research Council United Kingdom
Cdc20 Proteins, Nocodazole, Ubiquitin-Protein Ligases, Mitosis, Antineoplastic Agents, Cell Biology, Cell Cycle Checkpoints, Protein Serine-Threonine Kinases, HEK293 Cells, Humans, HeLa Cells
Cdc20 Proteins, Nocodazole, Ubiquitin-Protein Ligases, Mitosis, Antineoplastic Agents, Cell Biology, Cell Cycle Checkpoints, Protein Serine-Threonine Kinases, HEK293 Cells, Humans, HeLa Cells
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