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Ubiquitin and Parkinson's disease through the looking glass of genetics.

Abstract Biochemical alterations found in the brains of Parkinson's disease (PD) patients indicate that cellular stress is a major driver of dopaminergic neuronal loss. Oxidative stress, mitochondrial dysfunction, and ER stress lead to impairment of the homeostatic regulation of protein quality control pathways with a consequent increase in protein misfolding and aggregation and failure of the protein degradation machinery. Ubiquitin signalling plays a central role in protein quality control; however, prior to genetic advances, the detailed mechanisms of how impairment in the ubiquitin system was linked to PD remained mysterious. The discovery of mutations in the α-synuclein gene, which encodes the main protein misfolded in PD aggregates, together with mutations in genes encoding ubiquitin regulatory molecules, including PTEN-induced kinase 1 (PINK1), Parkin, and FBX07, has provided an opportunity to dissect out the molecular basis of ubiquitin signalling disruption in PD, and this knowledge will be critical for developing novel therapeutic strategies in PD that target the ubiquitin system.
PMID
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Authors

Mayor MeshTerms
Keywords

Parkinson's disease

kinase

ubiquitin

ubiquitin ligases

Journal Title the biochemical journal
Publication Year Start




PMID- 28408429
OWN - NLM
STAT- MEDLINE
DA  - 20170414
DCOM- 20170419
LR  - 20170419
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 474
IP  - 9
DP  - 2017 Apr 13
TI  - Ubiquitin and Parkinson's disease through the looking glass of genetics.
PG  - 1439-1451
LID - 10.1042/BCJ20160498 [doi]
AB  - Biochemical alterations found in the brains of Parkinson's disease (PD) patients 
      indicate that cellular stress is a major driver of dopaminergic neuronal loss.
      Oxidative stress, mitochondrial dysfunction, and ER stress lead to impairment of 
      the homeostatic regulation of protein quality control pathways with a consequent 
      increase in protein misfolding and aggregation and failure of the protein
      degradation machinery. Ubiquitin signalling plays a central role in protein
      quality control; however, prior to genetic advances, the detailed mechanisms of
      how impairment in the ubiquitin system was linked to PD remained mysterious. The 
      discovery of mutations in the alpha-synuclein gene, which encodes the main
      protein misfolded in PD aggregates, together with mutations in genes encoding
      ubiquitin regulatory molecules, including PTEN-induced kinase 1 (PINK1), Parkin, 
      and FBX07, has provided an opportunity to dissect out the molecular basis of
      ubiquitin signalling disruption in PD, and this knowledge will be critical for
      developing novel therapeutic strategies in PD that target the ubiquitin system.
CI  - (c) 2017 The Author(s).
FAU - Walden, Helen
AU  - Walden H
AD  - MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences,
      University of Dundee, Dundee, U.K. [email protected] [email protected]
FAU - Muqit, Miratul M K
AU  - Muqit MM
AD  - MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences,
      University of Dundee, Dundee, U.K. [email protected] [email protected]
AD  - School of Medicine, Dentistry & Nursing, University of Dundee, Dundee, U.K.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20170413
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Ubiquitin)
RN  - 0 (alpha-Synuclein)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
RN  - EC 2.3.2.27 (parkin protein)
SB  - IM
MH  - Animals
MH  - Humans
MH  - Oxidative Stress/physiology
MH  - Parkinson Disease/diagnosis/*genetics/*metabolism
MH  - Ubiquitin/*genetics/*metabolism
MH  - Ubiquitin-Protein Ligases/genetics/metabolism
MH  - alpha-Synuclein/genetics/metabolism
OTO - NOTNLM
OT  - Parkinson's disease
OT  - kinase
OT  - ubiquitin
OT  - ubiquitin ligases
EDAT- 2017/04/15 06:00
MHDA- 2017/04/20 06:00
CRDT- 2017/04/15 06:00
PHST- 2016/11/27 [received]
PHST- 2017/02/20 [revised]
PHST- 2017/02/20 [accepted]
AID - BCJ20160498 [pii]
AID - 10.1042/BCJ20160498 [doi]
PST - epublish
SO  - Biochem J. 2017 Apr 13;474(9):1439-1451. doi: 10.1042/BCJ20160498.

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