Cargando…

LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate

BACKGROUND: Lrrk2, a gene linked to Parkinson’s disease, encodes a large scaffolding protein with kinase and GTPase activities implicated in vesicle and cytoskeletal-related processes. At the presynaptic site, LRRK2 associates with synaptic vesicles through interaction with a panel of presynaptic pr...

Descripción completa

Detalles Bibliográficos
Autores principales:	Belluzzi, Elisa, Gonnelli, Adriano, Cirnaru, Maria-Daniela, Marte, Antonella, Plotegher, Nicoletta, Russo, Isabella, Civiero, Laura, Cogo, Susanna, Carrion, Maria Perèz, Franchin, Cinzia, Arrigoni, Giorgio, Beltramini, Mariano, Bubacco, Luigi, Onofri, Franco, Piccoli, Giovanni, Greggio, Elisa
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	BioMed Central 2016
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4711005/ https://www.ncbi.nlm.nih.gov/pubmed/26758690 http://dx.doi.org/10.1186/s13024-015-0066-z

Ejemplares similares

LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex
por: Cirnaru, Maria D., et al.
Publicado: (2014)

LRRK2 modulates neuronal vesicles cycle through protein interactions
por: Piccoli, Giovanni, et al.
Publicado: (2015)

Disassembly of All SNARE Complexes by N-Ethylmaleimide-sensitive Factor (NSF) Is Initiated by a Conserved 1:1 Interaction between α-Soluble NSF Attachment Protein (SNAP) and SNARE Complex
por: Vivona, Sandro, et al.
Publicado: (2013)

Ceramides in Parkinson’s Disease: From Recent Evidence to New Hypotheses
por: Plotegher, Nicoletta, et al.
Publicado: (2019)

Processive ATP-driven Substrate Disassembly by the N-Ethylmaleimide-sensitive Factor (NSF) Molecular Machine
por: Cipriano, Daniel J., et al.
Publicado: (2013)

Trafficking of the glutamate transporter is impaired in LRRK2-related Parkinson’s disease
por: Iovino, Ludovica, et al.
Publicado: (2022)

PAK6 Phosphorylates 14-3-3γ to Regulate Steady State Phosphorylation of LRRK2
por: Civiero, Laura, et al.
Publicado: (2017)

Divergent Effects of G2019S and R1441C LRRK2 Mutations on LRRK2 and Rab10 Phosphorylations in Mouse Tissues
por: Iannotta, Lucia, et al.
Publicado: (2020)

NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin
por: Choi, Ucheor B, et al.
Publicado: (2018)

Parkinson’s Disease–Associated LRRK2 Interferes with Astrocyte-Mediated Alpha-Synuclein Clearance
por: Streubel-Gallasch, Linn, et al.
Publicado: (2021)

The Role of the N-D1 Linker of the N-Ethylmaleimide-Sensitive Factor in the SNARE Disassembly
por: Liu, Cui-Cui, et al.
Publicado: (2013)

LRRK2 and neuroinflammation: partners in crime in Parkinson’s disease?
por: Russo, Isabella, et al.
Publicado: (2014)

Stimulation of NSF ATPase Activity by α-SNAP Is Required for SNARE Complex Disassembly and Exocytosis
por: Barnard, Richard J.O., et al.
Publicado: (1997)

Analysis of the Catecholaminergic Phenotype in Human SH-SY5Y and BE(2)-M17 Neuroblastoma Cell Lines upon Differentiation
por: Filograna, Roberta, et al.
Publicado: (2015)

Leucine-rich repeat kinase 2 and alpha-synuclein: intersecting pathways in the pathogenesis of Parkinson's disease?
por: Greggio, Elisa, et al.
Publicado: (2011)

Parkinson’s disease and immune system: is the culprit LRRKing in the periphery?
por: Greggio, Elisa, et al.
Publicado: (2012)

Pharmacological LRRK2 kinase inhibition induces LRRK2 protein destabilization and proteasomal degradation
por: Lobbestael, E., et al.
Publicado: (2016)

LRRK2 kinase activity regulates GCase level and enzymatic activity differently depending on cell type in Parkinson’s disease
por: Kedariti, Maria, et al.
Publicado: (2022)

Leucine‐rich repeat kinase 2 interacts with p21‐activated kinase 6 to control neurite complexity in mammalian brain
por: Civiero, Laura, et al.
Publicado: (2015)

GTP binding regulates cellular localization of Parkinson's disease-associated LRRK2
por: Blanca Ramírez, Marian, et al.
Publicado: (2017)

N-Ethylmaleimide Sensitive Factor (NSF) Inhibition Prevents Vascular Instability following Gram-Positive Pulmonary Challenge
por: Lee, Ji Young, et al.
Publicado: (2016)

The activity of Golgi transport vesicles depends on the presence of the N-ethylmaleimide-sensitive factor (NSF) and a soluble NSF attachment protein (alpha SNAP) during vesicle formation
Publicado: (1992)

Sequential SNARE disassembly and GATE-16–GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion
por: Müller, Joyce M.M., et al.
Publicado: (2002)

Structural principles of SNARE complex recognition by the AAA+ protein NSF
por: White, K Ian, et al.
Publicado: (2018)

Leucine-rich repeat kinase 2 positively regulates inflammation and down-regulates NF-κB p50 signaling in cultured microglia cells
por: Russo, Isabella, et al.
Publicado: (2015)

Erratum to: Leucine-rich repeat kinase 2 positively regulates inflammation and down-regulates NF-κB p50 signaling in cultured microglia cells
por: Russo, Isabella, et al.
Publicado: (2016)

Human SOD2 Modification by Dopamine Quinones Affects Enzymatic Activity by Promoting Its Aggregation: Possible Implications for Parkinson’s Disease
por: Belluzzi, Elisa, et al.
Publicado: (2012)

Levetiracetam treatment ameliorates LRRK2 pathological mutant phenotype
por: Rassu, Mauro, et al.
Publicado: (2019)

LRRK2 phosphorylation level correlates with abnormal motor behaviour in an experimental model of levodopa-induced dyskinesias
por: Stanic, Jennifer, et al.
Publicado: (2016)

Mechanistic insights into the SNARE complex disassembly
por: Huang, Xuan, et al.
Publicado: (2019)

The LRRK2 Variant E193K Prevents Mitochondrial Fission Upon MPP+ Treatment by Altering LRRK2 Binding to DRP1
por: Perez Carrion, Maria, et al.
Publicado: (2018)

Biochemical Characterization of Highly Purified Leucine-Rich Repeat Kinases 1 and 2 Demonstrates Formation of Homodimers
por: Civiero, Laura, et al.
Publicado: (2012)

Multiple factors maintain assembled trans-SNARE complexes in the presence of NSF and αSNAP
por: Prinslow, Eric A, et al.
Publicado: (2019)

Editorial: LRRK2—Fifteen Years From Cloning to the Clinic
por: Rideout, Hardy, et al.
Publicado: (2022)

LRRK2 Kinase Inhibition as a Therapeutic Strategy for Parkinson’s Disease, Where Do We Stand?
por: Taymans, Jean-Marc, et al.
Publicado: (2016)

Sensory deficit screen identifies nsf mutation that differentially affects SNARE recycling and quality control
por: Gao, Yan, et al.
Publicado: (2023)

Lysophosphatidylcholine inhibits membrane-associated SNARE complex disassembly
por: Shin, Leah, et al.
Publicado: (2012)

Comprehensive Structural and Thermodynamic Analysis of Prefibrillar WT α-Synuclein and Its G51D, E46K, and A53T Mutants by a Combination of Small-Angle X-ray Scattering and Variational Bayesian Weighting
por: Moretti, Paolo, et al.
Publicado: (2020)

Dynamics of SNARE Assembly and Disassembly during Sperm Acrosomal Exocytosis
por: Blas, Gerardo A. De, et al.
Publicado: (2005)

Genetic, Structural, and Molecular Insights into the Function of Ras of Complex Proteins Domains
por: Civiero, Laura, et al.
Publicado: (2014)

Cannot write session to /tmp/vufind_sessions/sess_vaj2qk0iuejqcbmlg598ns7cgr