Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin‐like domain

Sakata, Eri; Yamaguchi, Yoshiki; Kurimoto, Eiji; Kikuchi, Jun; Yokoyama, Shigeyuki; Yamada, Shingo; Kawahara, Hiroyuki; Yokosawa, Hideyoshi; Hattori, Nobutaka; Mizuno, Yoshikuni; Tanaka, Keiji; Kato, Koichi

doi:10.1038/sj.embor.embor764

Cited by 226 publications

(209 citation statements)

References 35 publications

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“…The low micromolar affinity constant measured between the Ubl and Rpn13 is in qualitative agreement with the NMR results. Moreover, the calculated K d between parkin Ubl and Rpn13 Pru domain is ϳ2 orders of magnitude lower than the one reported for parkin Ubl binding to the Rpn10 UIMs (217 Ϯ 51 M) (49), likely explaining the difficulty in confirming the parkin-Rpn10 interaction by pulldown assays (32). We could also show that the Ubl domain of parkin directly interacts with the active purified bovine proteasome (Fig.…”

Section: Resultsmentioning

confidence: 68%

“…Interestingly, Tsai et al (31) showed that the Ubl domain of parkin is necessary for its direct interaction with purified 26 S proteasomes in vitro. Additionally, two independent groups found that parkin could interact with the 26 S proteasome by binding the 19 S proteasome subunit Rpn10/S5a (32) or the 20 S subunit ␣4/PSMA7 (33). Although Rpn10 was shown to interact with the parkin Ubl domain (32), the C-terminal IBR-RING domain of parkin was found to interact with the C-terminal part of ␣4/PSMA7 (33).…”

mentioning

confidence: 99%

“…Additionally, two independent groups found that parkin could interact with the 26 S proteasome by binding the 19 S proteasome subunit Rpn10/S5a (32) or the 20 S subunit ␣4/PSMA7 (33). Although Rpn10 was shown to interact with the parkin Ubl domain (32), the C-terminal IBR-RING domain of parkin was found to interact with the C-terminal part of ␣4/PSMA7 (33). However, the precise mode of interaction between parkin and the proteasome remains to be determined.…”

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confidence: 99%

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The E3 Ubiquitin Ligase Parkin Is Recruited to the 26 S Proteasome via the Proteasomal Ubiquitin Receptor Rpn13

Aguileta

Korać

Durcan

et al. 2015

Journal of Biological Chemistry

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Background:The role of the N-terminal ubiquitin-like domain of the E3 ligase parkin is not fully understood. Results: Parkin is recruited to the 26 S proteasome through the interaction of its ubiquitin-like domain with the intrinsic proteasomal ubiquitin receptor Rpn13. Conclusion: Parkin turnover and E3 ligase activity can be regulated by its recruitment to the 26 S proteasome via Rpn13. Significance: Parkin-Rpn13 interaction might be exploited as a potential therapeutic strategy.

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Section: Resultsmentioning

confidence: 68%

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confidence: 99%

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confidence: 99%

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The E3 Ubiquitin Ligase Parkin Is Recruited to the 26 S Proteasome via the Proteasomal Ubiquitin Receptor Rpn13

Aguileta

Korać

Durcan

et al. 2015

Journal of Biological Chemistry

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“…As Herp has no demonstrable E3 ubiquitin-protein ligase activity, it is unlikely that Herp plays a direct role in protein substrate ubiquitination. On the other hand, the N-terminal ubiquitin-like domain of Herp may function as a proteasomeinteracting domain, as has recently been demonstrated for Parkin (52) and other ubiquitin-like domain-containing proteins (53). Our findings that ER-stressed cells overexpressing Herp exhibited reduced ER Ca 2ϩ release suggest that Herp may bind to and facilitate targeting of ER resident proteins involved in ER calcium regulation such as SERCA and the ER Ca 2ϩ release channels for proteasome-mediated degradation (54 -56).…”

Section: Discussionmentioning

confidence: 98%

Herp Stabilizes Neuronal Ca2+ Homeostasis and Mitochondrial Function during Endoplasmic Reticulum Stress

Chan

Zhang

et al. 2004

Journal of Biological Chemistry

114

147

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In response to endoplasmic reticulum (ER) stress, cells launch homeostatic and protective responses, but can also activate cell death cascades. A 54 kDa integral ER membrane protein called Herp was identified as a stress-responsive protein in non-neuronal cells. We report that Herp is present in neurons in the developing and adult brain, and that it is regulated in neurons by ER stress; sublethal levels of ER stress increase Herp levels, whereas higher doses decrease Herp levels and induce apoptosis. The endoplasmic reticulum (ER) 1 is a unique cellular compartment simultaneously involved in the processes of protein synthesis and Ca 2ϩ homeostasis. Various conditions, including oxidative and metabolic stress and Ca 2ϩ overload can interfere with ER functions leading to the accumulation of misfolded proteins. Cells sense and respond to such ER stress by activating a signaling cascade termed the unfolded protein response, which results in the transcriptional up-regulation of stress proteins including members of the glucose-regulated protein (grp) family and other protein chaperones (calnexin, calreticulin, ERp72) that enhance the protein folding capability of the ER (1). ER stress has been documented in neurons in a variety of acute pathological conditions including cerebral ischemia and severe epileptic seizures (2). However, despite the fact that disruption of cellular Ca 2ϩ homeostasis contributes to the death of neurons in these conditions, it is not known how molecular responses to ER stress modify cellular Ca 2ϩ homeostasis and the cell death process. Studies of cultured cells suggest that ER stress can stimulate the expression of cytoprotective genes such as protein chaperones (3) but may also trigger a form of programmed cell death called apoptosis (4), which may involve activation of ER-associated caspases and transcription factors such as Gadd153. A better understanding of ER stress and its links to cell survival/death decisions is therefore needed.Recent findings suggest that ER stress is also implicated in several chronic neurodegenerative disorders including Alzheimer's (5, 6), Parkinson's (7), and Huntington's (8) diseases. Alzheimer's disease (AD) results from altered proteolytic processing of the amyloid precursor protein (APP), resulting in aggregation of neurotoxic forms of amyloid ␤-peptide (A␤) (9). Exposure of cultured neurons to A␤-peptide, and metabolic and oxidative insults can induce an ER stress response (6, 10). Moreover, mutations in presenilin-1 (PS1) that cause earlyonset familial AD perturb ER Ca 2ϩ homeostasis (11, 12) and impair the ability of neurons to engage a cytoprotective ER stress response (20). The adverse effects of A␤ and PS1 mutations on ER function may sensitize neurons to excitotoxicity and apoptosis (11).A novel 54 kDa protein called Herp (homocysteine-induced ER protein) was recently identified and characterized as a stress-responsive protein localized in the ER membrane; Herp contains a ubiquitin-like domain and resembles the human DNA excision repair protein hHR23 ...

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“…The structural biology of ␣-synuclein has been resolved for several years: in solution it has little structure, being natively unfolded, but adopts a helical conformation on binding to lipid membranes. The structure of parkin is not yet solved apart from a small region at the N terminus, which has been recently described by using NMR (16), and hence there is still much work to be done on this protein.…”

Section: Fig 1 Similarities and Differences In Structures Of Differmentioning

confidence: 99%

Crystallizing ideas about Parkinson's disease

Cookson

2003

Proc. Natl. Acad. Sci. U.S.A.

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Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin‐like domain

Cited by 226 publications

References 35 publications

The E3 Ubiquitin Ligase Parkin Is Recruited to the 26 S Proteasome via the Proteasomal Ubiquitin Receptor Rpn13

The E3 Ubiquitin Ligase Parkin Is Recruited to the 26 S Proteasome via the Proteasomal Ubiquitin Receptor Rpn13

Herp Stabilizes Neuronal Ca2+ Homeostasis and Mitochondrial Function during Endoplasmic Reticulum Stress

Crystallizing ideas about Parkinson's disease

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