Mol Cell 2011 Aug;43(4):599-612
Department of Neurology, University of Michigan, Ann Arbor, MI 48109, USA.
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J Biol Chem 2013 Nov 8;288(48):34460-9. Epub 2013 Oct 8.
From the Departments of Pharmacology and Neurology and.
Deubiquitinases (DUBs) are proteases that regulate various cellular processes by controlling protein ubiquitination. Cell-based studies indicate that the regulation of the activity of DUBs is important for homeostasis and is achieved by multiple mechanisms, including through their own ubiquitination. However, the physiological significance of the ubiquitination of DUBs to their functions in vivo is unclear. Read More
Cell Mol Life Sci 2011 Jan 21;68(1):15-26. Epub 2010 Aug 21.
Department of Biomedical Science, CHA General Hospital, CHA University, 606-16 Yeoksam 1-Dong, Gangnam-Gu, Seoul, 135-081, Republic of Korea.
It has become apparent that ubiquitination plays a critical role in cell survival and cell death. In addition, deubiquitinating enzymes (DUBs) have been determined to be highly important regulators of these processes. Cells can be subjected to various stresses and respond in a variety of different ways ranging from activation of survival pathways to the promotion of cell death, which eventually eliminates damaged cells. Read More
Hum Mol Genet 2011 Jan 11;20(1):141-54. Epub 2010 Oct 11.
Centre for Neuronal Survival and McGill Parkinson Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.
Machado-Joseph disease (MJD), the most common dominantly inherited ataxia worldwide, is caused by a polyglutamine (polyQ) expansion in the deubiquitinating (DUB) enzyme ataxin-3. Interestingly, MJD can present clinically with features of Parkinsonism. In this study, we identify parkin, an E3 ubiquitin-ligase responsible for a common familial form of Parkinson's disease, as a novel ataxin-3 binding partner. Read More
Neurobiol Dis 2009 Mar 8;33(3):342-53. Epub 2008 Nov 8.
Graduate Program in Neuroscience and Medical Scientist Training Program, University of Iowa, 2206 MERF, Iowa City, IA 52242, USA.
Perturbations in neuronal protein homeostasis likely contribute to disease pathogenesis in polyglutamine (polyQ) neurodegenerative disorders. Here we provide evidence that the co-chaperone and ubiquitin ligase, CHIP (C-terminus of Hsp70-interacting protein), is a central component to the homeostatic mechanisms countering toxic polyQ proteins in the brain. Genetic reduction or elimination of CHIP accelerates disease in transgenic mice expressing polyQ-expanded ataxin-3, the disease protein in Spinocerebellar Ataxia Type 3 (SCA3). Read More