- Home
- Publications
- Publication Search
- Publication Details
Title
LRRK2 Promotes Tau Accumulation, Aggregation and Release
Authors
Keywords
LRRK2, Tau, Protein accumulation, Protein degradation
Journal
MOLECULAR NEUROBIOLOGY
Volume 53, Issue 5, Pages 3124-3135
Publisher
Springer Nature
Online
2015-05-26
DOI
10.1007/s12035-015-9209-z
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Differential protein-protein interactions of LRRK1 and LRRK2 indicate roles in distinct cellular signaling pathways
- (2014) Lauran Reyniers et al. JOURNAL OF NEUROCHEMISTRY
- PICALM modulates autophagy activity and tau accumulation
- (2014) Kevin Moreau et al. Nature Communications
- LRRK2 phosphorylates novel tau epitopes and promotes tauopathy
- (2013) Rachel M. Bailey et al. ACTA NEUROPATHOLOGICA
- Pathogenic Parkinson’s disease mutations across the functional domains of LRRK2 alter the autophagic/lysosomal response to starvation
- (2013) Claudia Manzoni et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Phosphorylation of Human Tau Protein by Microtubule Affinity-Regulating Kinase 2
- (2013) Martin Schwalbe et al. BIOCHEMISTRY
- Leucine-rich repeat kinase 2 regulates tau phosphorylation through direct activation of glycogen synthase kinase-3β
- (2013) Fumitaka Kawakami et al. FEBS Journal
- LRRK2 secretion in exosomes is regulated by 14-3-3
- (2013) K. B. Fraser et al. HUMAN MOLECULAR GENETICS
- A Direct Interaction between Leucine-rich Repeat Kinase 2 and Specific β-Tubulin Isoforms Regulates Tubulin Acetylation
- (2013) Bernard M. H. Law et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Regulation of Autophagy by LRRK2 in Caenorhabditis elegans
- (2013) Shamol Saha et al. Neurodegenerative Diseases
- Tau degradation: The ubiquitin–proteasome system versus the autophagy-lysosome system
- (2013) Min Jae Lee et al. PROGRESS IN NEUROBIOLOGY
- Tau Clearance Mechanisms and Their Possible Role in the Pathogenesis of Alzheimer Disease
- (2013) Adrianne S. Chesser et al. Frontiers in Neurology
- Role of LRRK2 kinase activity in the pathogenesis of Parkinson's disease
- (2012) Elisa Greggio BIOCHEMICAL SOCIETY TRANSACTIONS
- Presynaptic dysfunction in Parkinson's disease: a focus on LRRK2
- (2012) Elisa Belluzzi et al. BIOCHEMICAL SOCIETY TRANSACTIONS
- Degradation of tau protein by autophagy and proteasomal pathways: Figure 1
- (2012) Yipeng Wang et al. BIOCHEMICAL SOCIETY TRANSACTIONS
- Trans-cellular Propagation of Tau Aggregation by Fibrillar Species
- (2012) Najla Kfoury et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- LRRK2 interactions with α-synuclein in Parkinson’s disease brains and in cell models
- (2012) Patrícia Silva Guerreiro et al. JOURNAL OF MOLECULAR MEDICINE-JMM
- LRRK2 Phosphorylates Tubulin-Associated Tau but Not the Free Molecule: LRRK2-Mediated Regulation of the Tau-Tubulin Association and Neurite Outgrowth
- (2012) Fumitaka Kawakami et al. PLoS One
- High LRRK2 Levels Fail to Induce or Exacerbate Neuronal Alpha-Synucleinopathy in Mouse Brain
- (2012) Martin C. Herzig et al. PLoS One
- α-Synuclein Aggregation and Transmission Are Enhanced by Leucine-Rich Repeat Kinase 2 in Human Neuroblastoma SH-SY5Y Cells
- (2011) Kazunari Kondo et al. BIOLOGICAL & PHARMACEUTICAL BULLETIN
- Proteostasis of tau. Tau overexpression results in its secretion via membrane vesicles
- (2011) Diana Simón et al. FEBS LETTERS
- Association of LRRK2 exonic variants with susceptibility to Parkinson's disease: a case–control study
- (2011) Owen A Ross et al. LANCET NEUROLOGY
- Autophagic degradation of tau in primary neurons and its enhancement by trehalose
- (2011) Ulrike Krüger et al. NEUROBIOLOGY OF AGING
- The Parkinson's disease protein LRRK2 impairs proteasome substrate clearance without affecting proteasome catalytic activity
- (2011) M Lichtenberg et al. Cell Death & Disease
- 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization
- (2010) R. Jeremy Nichols et al. BIOCHEMICAL JOURNAL
- Mechanisms in dominant parkinsonism: The toxic triangle of LRRK2, α-synuclein, and tau
- (2010) Jean-Marc Taymans et al. BIOESSAYS
- The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease
- (2010) Mark R. Cookson NATURE REVIEWS NEUROSCIENCE
- Impaired dopaminergic neurotransmission and microtubule-associated protein tau alterations in human LRRK2 transgenic mice
- (2010) H.L. Melrose et al. NEUROBIOLOGY OF DISEASE
- Zooming into protein oligomerization in neurodegeneration using BiFC
- (2010) Susana A. Gonçalves et al. TRENDS IN BIOCHEMICAL SCIENCES
- Cerebrospinal Fluid β-Amyloid 42 and Tau Proteins as Biomarkers of Alzheimer-Type Pathologic Changes in the Brain
- (2009) Tero Tapiola et al. ARCHIVES OF NEUROLOGY
- Leucine-rich repeat kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease
- (2009) K. Venderova et al. HUMAN MOLECULAR GENETICS
- Leucine-rich repeat kinase 2 phosphorylates brain tubulin-beta isoforms and modulates microtubule stability - a point of convergence in Parkinsonian neurodegeneration?
- (2009) Frank Gillardon JOURNAL OF NEUROCHEMISTRY
- Phosphorylation of Ezrin/Radixin/Moesin Proteins by LRRK2 Promotes the Rearrangement of Actin Cytoskeleton in Neuronal Morphogenesis
- (2009) L. Parisiadou et al. JOURNAL OF NEUROSCIENCE
- The tau of MARK: a polarized view of the cytoskeleton
- (2009) Dorthe Matenia et al. TRENDS IN BIOCHEMICAL SCIENCES
- Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells
- (2008) Edward D. Plowey et al. JOURNAL OF NEUROCHEMISTRY
- The Roc domain of leucine-rich repeat kinase 2 is sufficient for interaction with microtubules
- (2008) Payal N. Gandhi et al. JOURNAL OF NEUROSCIENCE RESEARCH
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started