GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2 (Q24306167)

identical protein binding

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author

Elisa Greggio

6

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Alzbeta Trancikova

object named as

Alzbeta Trancikova

2

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Luigi Bubacco

object named as

Luigi Bubacco

5

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Liliane Glauser

4

object named as

Liliane Glauser

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author name string

Alice Biosa

1

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Laura Civiero

3

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Darren J Moore

Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control study

7

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language of work or name

English

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publication date

15 March 2013

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published in

Human Molecular Genetics

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volume

22

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issue

6

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page(s)

1140-56

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cites work

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GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease

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The R1441C mutation of LRRK2 disrupts GTP hydrolysis

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Kinase activity of mutant LRRK2 mediates neuronal toxicity

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Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity

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GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1

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GTPase activity plays a key role in the pathobiology of LRRK2.

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

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

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

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LRRK2 kinase activity is dependent on LRRK2 GTP binding capacity but independent of LRRK2 GTP binding

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Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase

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Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation

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The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation

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Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization

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The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation

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The familial Parkinsonism gene LRRK2 regulates neurite process morphology

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Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis

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Chemoproteomics-based design of potent LRRK2-selective lead compounds that attenuate Parkinson's disease-related toxicity in human neurons

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Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2.

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The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites

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Identification of the autophosphorylation sites of LRRK2.

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Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities

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Structure-function relationships of the G domain, a canonical switch motif

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It takes two to tango: regulation of G proteins by dimerization

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ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2

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Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells

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LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice

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

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