Global changes to the ubiquitin system in Huntington's disease

Eric J. Bennett, Thomas A. Shaler, Ben Woodman, Kwon-Yul Ryu, Tatiana S. Zaitseva, Christopher H. Becker, Gillian P. Bates, Howard Schulman and Ron R. Kopito ()
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Eric J. Bennett: Stanford University, Stanford, California 94305, USA
Thomas A. Shaler: PPD Biomarker Discovery Inc., 1505 O’Brien Drive, Menlo Park, California 94025, USA
Ben Woodman: King’s College London School of Medicine, London SE1 9RT, UK
Kwon-Yul Ryu: Stanford University, Stanford, California 94305, USA
Tatiana S. Zaitseva: Stanford University, Stanford, California 94305, USA
Christopher H. Becker: PPD Biomarker Discovery Inc., 1505 O’Brien Drive, Menlo Park, California 94025, USA
Gillian P. Bates: King’s College London School of Medicine, London SE1 9RT, UK
Howard Schulman: PPD Biomarker Discovery Inc., 1505 O’Brien Drive, Menlo Park, California 94025, USA
Ron R. Kopito: Stanford University, Stanford, California 94305, USA

Nature, 2007, vol. 448, issue 7154, 704-708

Abstract: Ubiquitin inclusions In patients with the neurodegenerative disorder Huntington's disease, the neurons contain abnormal protein inclusion bodies enriched with ubiquitin. It has been suggested that alterations in the cellular ubiquitination and proteasomal degradation system contribute to the disease. A mass spectrometry analysis of the brains of Huntington's disease patients and of several mouse models of the disease confirms that ubiquitin chains are ever-present in protein inclusions, suggesting that a general dysfunction of this system may contribute to the disease process. These observations point to ubiquitin as possible diagnostic tool, and since abnormal enrichment of ubiquitin in neuropathological lesions is also a feature of Alzheimer's disease, it may be that these neurologically diverse diseases share fundamental molecular features.

Date: 2007
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DOI: 10.1038/nature06022

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