Ankyrin repeat and BTB/POZ domain containing protein-2 inhibits the aggregation of alpha-synuclein: implications for Parkinson's disease

FEBS Lett. 2013 Nov 1;587(21):3567-74. doi: 10.1016/j.febslet.2013.09.020. Epub 2013 Sep 25.

Abstract

Aggregation of α-synuclein is a pathological hallmark of sporadic or familial PD. However, the detailed molecular mechanism responsible for the aggregation of α-synuclein has not been properly explored. In the present study, we have identified a novel role of an anti-tumorigenic BTB/POZ domain containing protein-2 (BPOZ-2) in the regulation of α-synuclein accumulation in dopaminergic (DA) neurons. MPP(+), an etiological factor for PD, significantly downregulated the expression of BPOZ-2 ahead of α-synuclein upregulation. Moreover, siRNA knockdown of BPOZ-2 alone stimulated the aggregation of α-synuclein protein; the effect was further induced in presence of MPP(+) in mouse primary DA neurons. Finally, the absence of BPOZ-2 in α-synuclein expressing neuronal populations of MPTP-intoxicated mouse and primate nigra indicates that the suppression of BPOZ-2 could be involved in the accumulation of α-synuclein protein.

Keywords: ABTB2; BPOZ-2; Neuron; α-Synuclein.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Ankyrin Repeat*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Down-Regulation
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Neurons / metabolism
  • Nuclear Proteins
  • Parkinson Disease / metabolism*
  • RNA, Small Interfering / metabolism
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*
  • alpha-Synuclein / antagonists & inhibitors*
  • alpha-Synuclein / metabolism*

Substances

  • Abtb2 protein, mouse
  • DNA-Binding Proteins
  • Nuclear Proteins
  • RNA, Small Interfering
  • Repressor Proteins
  • alpha-Synuclein