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Ankyrin repeat and BTB/POZ domain containing protein‐2 inhibits the aggregation of alpha‐synuclein: Implications for Parkinson's disease
Author(s) -
Roy Avik,
Pahan Kalipada
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.09.020
Subject(s) - alpha synuclein , downregulation and upregulation , synuclein , ankyrin repeat , gene knockdown , protein aggregation , chemistry , ankyrin , microbiology and biotechnology , dopaminergic , parkinson's disease , biology , neuroscience , dopamine , biochemistry , disease , medicine , gene
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.