Details

Autor(en) / Beteiligte

• Kelly J. Inglis
• David Chereau
• Elizabeth F. Brigham
• San-San Chiou
• Susanne Schöbel
• Normand L. Frigon
• Mei Yu
• Russell J. Caccavello
• Seth Nelson
• Ruth Motter
• Sarah Wright
• David Chian
• Pamela Santiago
• Ferdie Soriano
• Carla Ramos
• Kyle Powell
• Jason M. Goldstein
• Michael Babcock
• Ted Yednock
• Frederique Bard
• Guriqbal S. Basi
• Hing Sham
• Tamie J. Chilcote
• Lisa McConlogue
• Irene Griswold-Prenner
• John P. Anderson

Titel

Polo-like Kinase 2 (PLK2) Phosphorylates α-Synuclein at Serine 129 in Central Nervous System

Ist Teil von

• The Journal of biological chemistry, 2009-01, Vol.284 (5), p.2598

Ort / Verlag

American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

2009

Quelle

Electronic Journals Library

Beschreibungen/Notizen

• Several neurological diseases, including Parkinson disease and dementia with Lewy bodies, are characterized by the accumulation of α-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 α-synuclein phosphorylation at Ser-129 in neurons. PLK2 directly phosphorylates α-synuclein at Ser-129 in an in vitro biochemical assay. Inhibitors of PLK kinases inhibited α-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 α-synuclein phosphorylation in central nervous system.