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Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system.

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.

Pubmed ID: 19004816

Authors

  • Inglis KJ
  • Chereau D
  • Brigham EF
  • Chiou SS
  • Schöbel S
  • Frigon NL
  • Yu M
  • Caccavello RJ
  • Nelson S
  • Motter R
  • Wright S
  • Chian D
  • Santiago P
  • Soriano F
  • Ramos C
  • Powell K
  • Goldstein JM
  • Babcock M
  • Yednock T
  • Bard F
  • Basi GS
  • Sham H
  • Chilcote TJ
  • McConlogue L
  • Griswold-Prenner I
  • Anderson JP

Journal

The Journal of biological chemistry

Publication Data

January 30, 2009

Associated Grants

None

Mesh Terms

  • Animals
  • Base Sequence
  • Cell Line
  • Central Nervous System
  • DNA Primers
  • Enzyme-Linked Immunosorbent Assay
  • Humans
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Phosphorylation
  • Protein Kinases
  • Protein-Serine-Threonine Kinases
  • RNA Interference
  • Serine
  • alpha-Synuclein