Mutations in the parkin gene are a common cause of autosomal recessive early-onset parkinsonism. Parkin functions as an E3 ubiquitin ligase where it can polyubiquitinate a number of its protein substrates, thus targeting them for degradation by the 26 S proteasomal complex. Recent studies have demonstrated that alternative modes of parkin-mediated ubiquitination may serve other non-degradative regulatory roles. In addition, parkin appears to function as a multipurpose neuroprotectant in a number of toxic paradigms. Coupled with these observations, parkin may integrate other gene products associated with parkinsonism, including α-synuclein, LRRK2 (leucine-rich repeat kinase 2), DJ-1 and PINK1 [PTEN (phosphatase and tensin homologue deleted on chromosome 10)-induced putative kinase 1], into a common biochemical pathway of potential relevance to disease pathogenesis. Parkin therefore represents a unique multifaceted ubiquitin ligase consistent with an important housekeeping role in maintaining the integrity or survival of dopaminergic neurons.
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October 2006
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Conference Article|
October 25 2006
Parkin: a multifaceted ubiquitin ligase
D.J. Moore
D.J. Moore
1
1Institute for Cell Engineering and Department of Neurology, Johns Hopkins University School of Medicine, 733 North Broadway, Broadway Research Building, Suite 731, Baltimore, MD 21205, U.S.A.
1email dmoore20@jhmi.edu
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Publisher: Portland Press Ltd
Received:
July 17 2006
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2006 The Biochemical Society
2006
Biochem Soc Trans (2006) 34 (5): 749–753.
Article history
Received:
July 17 2006
Citation
D.J. Moore; Parkin: a multifaceted ubiquitin ligase. Biochem Soc Trans 1 October 2006; 34 (5): 749–753. doi: https://doi.org/10.1042/BST0340749
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