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PINK1 rendered temperature sensitive by disease-associated and engineered mutations.
scientific article published on 3 March 2013
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Europe PubMed Central
PMC publication ID
3674799
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23459931%20AND%20SRC:MED&resulttype=core&format=json
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24 February 2020
title
PINK1 rendered temperature sensitive by disease-associated and engineered mutations
(English)
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3674799
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24 February 2020
author
Chunxin Wang
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2
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3674799
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24 February 2020
John E. Walker
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4
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3674799
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24 February 2020
Richard J. Youle
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Richard J Youle
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3674799
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24 February 2020
Derek P Narendra
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Derek P Narendra
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3674799
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24 February 2020
publication date
3 March 2013
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Europe PubMed Central
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3674799
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24 February 2020
published in
Human Molecular Genetics
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Europe PubMed Central
PMC publication ID
3674799
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23459931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
24 February 2020
volume
22
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3674799
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24 February 2020
issue
13
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PMC publication ID
3674799
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24 February 2020
page(s)
2572-2589
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3674799
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retrieved
24 February 2020
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PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
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PubMed Central
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PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
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Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations.
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29 September 2017
Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin
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Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy
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Targeting mitochondrial dysfunction: role for PINK1 and Parkin in mitochondrial quality control
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Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
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DJ-1 acts in parallel to the PINK1/parkin pathway to control mitochondrial function and autophagy
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29 September 2017
p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
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29 September 2017
p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria
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29 September 2017
Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update
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29 September 2017
PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
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29 September 2017
The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway
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29 September 2017
Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
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29 September 2017
PINK1 is selectively stabilized on impaired mitochondria to activate Parkin
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29 September 2017
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
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29 September 2017
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
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Structure of the Pseudokinase VRK3 Reveals a Degraded Catalytic Site, a Highly Conserved Kinase Fold, and a Putative Regulatory Binding Site
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Drosophila protein kinase CK2 is rendered temperature-sensitive by mutations of highly conserved residues flanking the activation segment.
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29 September 2017
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
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Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1.
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Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
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Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein
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Three-dimensional structure of mammalian casein kinase I: molecular basis for phosphate recognition
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Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism.
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2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor
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Identifiers
DOI
10.1093/HMG/DDT106
1 reference
stated in
Europe PubMed Central
PMC publication ID
3674799
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23459931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
24 February 2020
PMC publication ID
3674799
1 reference
stated in
Europe PubMed Central
PMC publication ID
3674799
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23459931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
24 February 2020
PubMed publication ID
23459931
1 reference
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Europe PubMed Central
PMC publication ID
3674799
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23459931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
24 February 2020
ResearchGate publication ID
235787175
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