| First Author | Roy A | Year | 2013 |
| Journal | FEBS Lett | Volume | 587 |
| Issue | 21 | Pages | 3567-74 |
| PubMed ID | 24076025 | Mgi Jnum | J:202009 |
| Mgi Id | MGI:5516416 | Doi | 10.1016/j.febslet.2013.09.020 |
| Citation | Roy A, et al. (2013) Ankyrin repeat and BTB/POZ domain containing protein-2 inhibits the aggregation of alpha-synuclein: Implications for Parkinson's disease. FEBS Lett 587(21):3567-74 |
| abstractText | Aggregation of alpha-synuclein is a pathological hallmark of sporadic or familial PD. However, the detailed molecular mechanism responsible for the aggregation of alpha-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 alpha-synuclein accumulation in dopaminergic (DA) neurons. MPP(+), an etiological factor for PD, significantly downregulated the expression of BPOZ-2 ahead of alpha-synuclein upregulation. Moreover, siRNA knockdown of BPOZ-2 alone stimulated the aggregation of alpha-synuclein protein; the effect was further induced in presence of MPP(+) in mouse primary DA neurons. Finally, the absence of BPOZ-2 in alpha-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 alpha-synuclein protein. |
