14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization (Q24339094)

2

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Alan R. Prescott

object named as

Alan R Prescott

10

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Dario Alessi

object named as

Dario R Alessi

11

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author name string

R Jeremy Nichols

1

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Nicholas A Morrice

3

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David G Campbell

4

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Alban Ordureau

6

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Thomas Macartney

7

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Youren Tong

8

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Jie Shen

Creative Commons Attribution-NonCommercial 2.5 Generic

9

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language of work or name

English

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publication date

15 September 2010

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published in

Biochemical Journal

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volume

430

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issue

3

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page(s)

393-404

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copyright license

start time

6 May 2020

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model

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Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration

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Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity

19 March 2017

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14-3-3eta is a novel regulator of parkin ubiquitin ligase

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Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology

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Regulation of the polarity kinases PAR-1/MARK by 14-3-3 interaction and phosphorylation

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Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase III beta protects from dephosphorylation and stabilizes lipid kinase activity

19 March 2017

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LRRK2 in Parkinson's disease: protein domains and functional insights

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Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease

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alpha-Synuclein shares physical and functional homology with 14-3-3 proteins

19 March 2017

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LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity

7 April 2017

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Kinase activity is required for the toxic effects of mutant LRRK2/dardarin

7 April 2017

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Differential neuroprotective effects of 14-3-3 proteins in models of Parkinson's disease.

7 April 2017

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Reevaluation of phosphorylation sites in the Parkinson disease-associated leucine-rich repeat kinase 2

27 September 2017

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Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease

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R1441C mutation in LRRK2 impairs dopaminergic neurotransmission in mice.

27 September 2017

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27 September 2017

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The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2.

27 September 2017

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27 September 2017

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Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.

27 September 2017

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14-3-3 proteins in the nervous system

27 September 2017

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27 September 2017

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27 September 2017

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14-3-3 protein is a component of Lewy bodies in Parkinson's disease-mutation analysis and association studies of 14-3-3 eta.

30 May 2018

1 reference

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Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding

29 November 2018

1 reference

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Comprehensive analysis of LRRK2 in publicly available Parkinson's disease cases and neurologically normal controls

29 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/20642453

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteins

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/20642453

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1042/BJ20100483

1 reference

1364133

1364133

1 reference

1 reference

1 reference