Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system.
J Biol Chem
; 284(5): 2598-2602, 2009 Jan 30.
Article
in En
| MEDLINE
| ID: mdl-19004816
ABSTRACT
Several neurological diseases, including Parkinson disease and dementia with Lewy bodies, are characterized by the accumulation of alpha-synuclein phosphorylated at Ser-129 (p-Ser-129). The kinase or kinases responsible for this phosphorylation have been the subject of intense investigation. Here we submit evidence that polo-like kinase 2 (PLK2, also known as serum-inducible kinase or SNK) is a principle contributor to alpha-synuclein phosphorylation at Ser-129 in neurons. PLK2 directly phosphorylates alpha-synuclein at Ser-129 in an in vitro biochemical assay. Inhibitors of PLK kinases inhibited alpha-synuclein phosphorylation both in primary cortical cell cultures and in mouse brain in vivo. Finally, specific knockdown of PLK2 expression by transduction with short hairpin RNA constructs or by knock-out of the plk2 gene reduced p-Ser-129 levels. These results indicate that PLK2 plays a critical role in alpha-synuclein phosphorylation in central nervous system.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Kinases
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Serine
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Central Nervous System
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Alpha-Synuclein
Limits:
Animals
/
Humans
Language:
En
Journal:
J Biol Chem
Year:
2009
Document type:
Article