14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

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14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization is …
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scholarly articleQ13442814

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P356DOI10.1042/BJ20100483
P3181OpenCitations bibliographic resource ID1364133
P932PMC publication ID2932554
P698PubMed publication ID20642453
P5875ResearchGate publication ID45273677

P50authorDario AlessiQ5222818
Nicolas DzamkoQ57321778
Maria DeakQ28357878
Alan R. PrescottQ37646420
P2093author name stringJie Shen
David G Campbell
Nicholas A Morrice
Thomas Macartney
Youren Tong
Alban Ordureau
R Jeremy Nichols
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LRRK2 exon 41 mutations in sporadic Parkinson disease in EuropeansQ42165517
Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 bindingQ44151283
14-3-3 protein is a component of Lewy bodies in Parkinson's disease-mutation analysis and association studies of 14-3-3 eta.Q44247686
Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteinsQ77790311
Comprehensive analysis of LRRK2 in publicly available Parkinson's disease cases and neurologically normal controlsQ80535570
Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activityQ22254785
Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degenerationQ24298689
The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sitesQ24313336
Differential 14-3-3 affinity capture reveals new downstream targets of phosphatidylinositol 3-kinase signalingQ24319111
LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular modelQ24656256
14-3-3eta is a novel regulator of parkin ubiquitin ligaseQ28115387
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathologyQ28131833
alpha-Synuclein shares physical and functional homology with 14-3-3 proteinsQ28139698
LRRK2 in Parkinson's disease: protein domains and functional insightsQ28235024
Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase III beta protects from dephosphorylation and stabilizes lipid kinase activityQ28258031
Regulation of the polarity kinases PAR-1/MARK by 14-3-3 interaction and phosphorylationQ28263242
Cloning of the gene containing mutations that cause PARK8-linked Parkinson's diseaseQ28292932
The Structural Basis for 14-3-3:Phosphopeptide Binding SpecificityQ29547190
MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantificationQ29547200
Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control studyQ29614953
LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activityQ29615144
Kinase activity is required for the toxic effects of mutant LRRK2/dardarinQ29620478
R1441C mutation in LRRK2 impairs dopaminergic neurotransmission in mice.Q30483115
14-3-3 proteins in the nervous systemQ33188355
Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1.Q33292483
The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2.Q33292556
Reevaluation of phosphorylation sites in the Parkinson disease-associated leucine-rich repeat kinase 2Q34121655
Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.Q35787179
Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's diseaseQ37139305
Zeroing in on LRRK2-linked pathogenic mechanisms in Parkinson's disease.Q37313530
LRRK2 in Parkinson's disease: biochemical functionsQ37608633
Differential neuroprotective effects of 14-3-3 proteins in models of Parkinson's disease.Q39620800
P275copyright licenseCreative Commons Attribution-NonCommercial 2.5 GenericQ19113746
P6216copyright statuscopyrightedQ50423863
P433issue3
P407language of work or nameEnglishQ1860
P921main subjectcell biologyQ7141
Parkinson's diseaseQ11085
P304page(s)393-404
P577publication date2010-09-15
P1433published inBiochemical JournalQ864221
P1476title14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization
P478volume430

Reverse relations

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