Document Detail


Ubiquitination of alpha-synuclein.
MedLine Citation:
PMID:  15628878     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Filamentous alpha-synuclein depositions are the defining hallmarks of a subset of neurodegenerative diseases including Parkinson's disease (PD), dementia with Lewy bodies, and multiple system atrophy. We previously reported that alpha-synuclein in those brains are extensively phosphorylated at Ser129 [Fujiwara et al. (2002) Nat. Cell Biol. 4, 160-164] and also partially ubiquitinated [Hasegawa et al. (2002) J. Biol. Chem. 277, 49071-49076]. Here, we investigate ubiquitination of alpha-synuclein in vitro and in vivo and report the ubiquitination sites and the effects of familial PD-linked mutations, phosphorylation, and fibril formation on ubiquitination. Protein-sequence analysis revealed that Lys21, Lys23, Lys32, and Lys34 within the repeats in the amino-terminal half are liable to ubiquitination in vitro. A site-directed mutagensis study confirmed that these are the major ubiquitination sites. A53T and A30P mutations had no significant effect on ubiquitination. Similarly, phosphorylation of alpha-synuclein at Ser129 did not affect ubiquitination. Notably, we show that assembled, filamentous alpha-synuclein is less ubiquitinated than the soluble form and that the major ubiquitination sites are localized to Lys6, Lys10, and Lys12 at the amino-terminal region of filamentous alpha-synuclein. Furthermore, we successfully detected ubiquitination of alpha-synuclein in 293T cells by cotransfection with alpha-synuclein and ubiquitin. The in vivo ubiquitination sites were found to be identical to those in filamentous alpha-synuclein. PD-linked mutations and phosphorylation at Ser129 had no effects on ubiquitination of alpha-synuclein in vivo. These data may have implications for the mechanisms of the formation of alpha-synuclein deposits in alpha-synucleinopathy brains.
Authors:
Takashi Nonaka; Takeshi Iwatsubo; Masato Hasegawa
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  44     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  2005 Jan 
Date Detail:
Created Date:  2005-01-04     Completed Date:  2005-03-04     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  361-8     Citation Subset:  IM    
Affiliation:
Department of Molecular Neurobiology, Tokyo Institute of Psychiatry, Tokyo Metropolitan Organization for Medical Research, 2-1-8 Kamikitazawa, Setagaya-ku, Tokyo 156-8585, Japan.
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MeSH Terms
Descriptor/Qualifier:
Binding Sites
Brain / metabolism
Cell Line
Humans
Kidney
Mutation
Nerve Tissue Proteins / metabolism*
Parkinson Disease / genetics
Synucleins
Ubiquitin / chemistry,  genetics*,  metabolism*
alpha-Synuclein
Chemical
Reg. No./Substance:
0/Nerve Tissue Proteins; 0/SNCA protein, human; 0/Synucleins; 0/Ubiquitin; 0/alpha-Synuclein

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