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Imai, Y, Soda, M, Inoue, H, Hattori, N, Mizuno, Y and Takahashi, R (2001) An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105:891-902
A putative G protein-coupled transmembrane polypeptide, named Pael receptor, was identified as an interacting protein with Parkin, a gene product responsible for autosomal recessive juvenile Parkinsonism (AR-JP). When overexpressed in cells, this receptor tends to become unfolded, insoluble, and ubiquitinated in vivo. The insoluble Pael receptor leads to unfolded protein-induced cell death. Parkin specifically ubiquitinates this receptor in the presence of ubiquitin-conjugating enzymes resident in the endoplasmic reticulum and promotes the degradation of insoluble Pael receptor, resulting in suppression of the cell death induced by Pael receptor overexpression. Moreover, the insoluble form of Pael receptor accumulates in the brains of AR-JP patients. Here, we show that the unfolded Pael receptor is a substrate of Parkin, the accumulation of which may cause selective neuronal death in AR-JP.
Acetylcysteine/analogs & derivatives; Acetylcysteine/pharmacology; Brain/cytology; Brain/metabolism; Cell Death; Cells, Cultured; Cysteine Proteinase Inhibitors/pharmacology; Endoplasmic Reticulum/metabolism; Humans; Ligases/genetics; Ligases/metabolism; Microscopy, Fluorescence; Parkinsonian Disorders/genetics; Parkinsonian Disorders/metabolism; Precipitin Tests; Protein Binding; Protein Folding; Receptors, Cell Surface/genetics; Receptors, Cell Surface/metabolism; Recombinant Fusion Proteins/metabolism; Two-Hybrid System Techniques; Ubiquitin-Conjugating Enzymes; Ubiquitin-Protein Ligases; Ubiquitins/metabolism