Ubiquitin–proteasome-mediated cyclin C degradation promotes cell survival following nitrogen starvation
Stephen D. Willis, Sara E. Hanley, Thomas Beishke, Prasanna Tati, Katrina F. Cooper
Abstract
allows enhanced cell growth under mild starvation. However, unlike oxidative stress, cyclin C is destroyed prior to its cytoplasmic translocation. This is important as targeting cyclin C to the mitochondria induces both mitochondrial fragmentation and cell death following nitrogen starvation. These results indicate that cyclin C destruction pathways are fine tuned depending on the stress and that its terminal subcellular address influences the decision between initiating cell death or cell survival pathways.
Topics & Concepts
BiologyProteasomeUbiquitinCell biologyDegradation (telecommunications)Ubiquitin ligaseStarvationProtein degradationCell cycleBiochemistryCellEndocrinologyTelecommunicationsComputer scienceGeneUbiquitin and proteasome pathwaysGenetics and Neurodevelopmental DisordersAutophagy in Disease and Therapy