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Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Imai, Yuzuru Soda, Mariko Takahashi, Ryosuke |
| Copyright Year | 2000 |
| Abstract | Autosomal recessive juvenile parkinsonism (AR-JP) is caused by mutations in the parkin gene. Parkin protein is characterized by a ubiquitin-like domain at its NH(2)-terminus and two RING finger motifs and an IBR (in between RING fingers) at its COOH terminus (RING-IBR-RING). Here, we show that Parkin is a RING-type E3 ubiquitin-protein ligase which binds to E2 ubiquitin-conjugating enzymes, including UbcH7 and UbcH8, through its RING-IBR-RING motif. Moreover, we found that unfolded protein stress induces up-regulation of both the mRNA and protein level of Parkin. Furthermore, overexpression of Parkin, but not a set of mutants without the E3 activity, specifically suppressed unfolded protein stress-induced cell death. These findings demonstrate that Parkin is an E3 enzyme and suggest that it is involved in the ubiquitination pathway for misfolded proteins derived from endoplasmic reticulum and contributes to protection from neurotoxicity induced by unfolded protein stresses. |
| Starting Page | 278 |
| Ending Page | 281 |
| Page Count | 4 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://huguenardlab.stanford.edu/205/imai.pdf |
| PubMed reference number | 10973942v1 |
| Volume Number | 275 |
| Issue Number | 46 |
| Journal | The Journal of biological chemistry |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Cell Death Endoplasmic Reticulum Fingers Mutation Neurotoxicity Syndromes PARK2 gene Parkinsonian Disorders Protein Domain Retinoschisis, Juvenile, X-Linked Ubiquitination Up-Regulation (Physiology) mutant ubiquitin-protein ligase |
| Content Type | Text |
| Resource Type | Article |
