Cargando…

Membrane Binding of α-Synuclein Stimulates Expansion of SNARE-Dependent Fusion Pore

SNARE-dependent membrane fusion is essential for neurotransmitter release at the synapse. Recently, α-synuclein has emerged as an important regulator for membrane fusion. Misfolded α-synuclein oligomers are potent fusion inhibitors. However, the function of normal α-synuclein has been elusive. Here,...

Descripción completa

Detalles Bibliográficos
Autores principales:	Khounlo, Ryan, Hawk, Brenden J. D., Khu, Tung-Mei, Yoo, Gyeongji, Lee, Nam Ki, Pierson, Josh, Shin, Yeon-Kyun
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Frontiers Media S.A. 2021
Materias:	Cell and Developmental Biology
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8326570/ https://www.ncbi.nlm.nih.gov/pubmed/34350173 http://dx.doi.org/10.3389/fcell.2021.663431

Ejemplares similares

Alpha-Synuclein Continues to Enhance SNARE-Dependent Vesicle Docking at Exorbitant Concentrations
por: Hawk, Brenden J. D., et al.
Publicado: (2019)

Stabilization of the SNARE Core by Complexin-1 Facilitates Fusion Pore Expansion
por: Pierson, Josh, et al.
Publicado: (2021)

Cooperative inhibition of SNARE-mediated vesicle fusion by α-synuclein monomers and oligomers
por: Yoo, Gyeongji, et al.
Publicado: (2021)

α-Synuclein Disrupts Vesicle Fusion by Two Mutant-Specific Mechanisms
por: Yoo, Gyeongji, et al.
Publicado: (2022)

Dilation of fusion pores by crowding of SNARE proteins
por: Wu, Zhenyong, et al.
Publicado: (2017)

α-Synuclein is required for sperm exocytosis at a post-fusion stage
por: Buzzatto, Micaela Vanina, et al.
Publicado: (2023)

Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion
por: Lu, Xiaobing, et al.
Publicado: (2008)

Regulation of Exocytotic Fusion Pores by SNARE Protein Transmembrane Domains
por: Wu, Zhenyong, et al.
Publicado: (2017)

ER-PM Contact Sites – SNARING Actors in Emerging Functions
por: Hewlett, Bailey, et al.
Publicado: (2021)

The Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex Regulation
por: Dubuke, Michelle L., et al.
Publicado: (2016)

Activity of the SNARE Protein SNAP29 at the Endoplasmic Reticulum and Golgi Apparatus
por: Morelli, Elena, et al.
Publicado: (2021)

Role of SNAREs in Unconventional Secretion—Focus on the VAMP7-Dependent Secretion
por: Vats, Somya, et al.
Publicado: (2022)

Nonaggregated α-Synuclein Influences SNARE-Dependent Vesicle Docking via Membrane Binding
por: Lai, Ying, et al.
Publicado: (2014)

Dual Effects of Presynaptic Membrane Mimetics on α-Synuclein Amyloid Aggregation
por: Lin, Yuxi, et al.
Publicado: (2022)

The Lack of SNARE Protein Homolog Syn8 Influences Biofilm Formation of Candida glabrata
por: Chen, Xinyue, et al.
Publicado: (2021)

Exocytotic pore in a SNARE
por: Jorgačevski, Jernej, et al.
Publicado: (2017)

α-Synuclein Promotes Dilation of the Exocytotic Fusion Pore
por: Logan, Todd, et al.
Publicado: (2017)

Nanodisc-cell fusion: control of fusion pore nucleation and lifetimes by SNARE protein transmembrane domains
por: Wu, Zhenyong, et al.
Publicado: (2016)

GARP dysfunction results in COPI displacement, depletion of Golgi v-SNAREs and calcium homeostasis proteins
por: Khakurel, Amrita, et al.
Publicado: (2022)

Trans-SNARE complex dynamics and number determine nascent fusion pore properties
por: Bao, Huan, et al.
Publicado: (2018)

Vesicular control of fusion pore expansion
por: Neuland, Kathrin, et al.
Publicado: (2015)

The Role of Lipids in the Initiation of α-Synuclein Misfolding
por: Kiechle, Martin, et al.
Publicado: (2020)

Intracellular Alpha-Synuclein and Immune Cell Function
por: Grozdanov, Veselin, et al.
Publicado: (2020)

The Role of Glial Mitochondria in α-Synuclein Toxicity
por: Jeon, Yu-Mi, et al.
Publicado: (2020)

Editorial: Intracellular Mechanisms of α-Synuclein Processing
por: Zunke, Friederike, et al.
Publicado: (2021)

The SNARE protein Vti1b is recruited to the sites of BCR activation but is redundant for antigen internalisation, processing and presentation
por: Music, Amna, et al.
Publicado: (2022)

Reversal of Alpha-Synuclein Fibrillization by Protein Disulfide Isomerase
por: Serrano, Albert, et al.
Publicado: (2020)

“Janus-Faced” α-Synuclein: Role in Parkinson’s Disease
por: Ray, Bipul, et al.
Publicado: (2021)

The neuronal calcium sensor Synaptotagmin-1 and SNARE proteins cooperate to dilate fusion pores
por: Wu, Zhenyong, et al.
Publicado: (2021)

SNARE zippering
por: Lou, Xiaochu, et al.
Publicado: (2016)

Linking Alpha-Synuclein to the Actin Cytoskeleton: Consequences to Neuronal Function
por: Oliveira da Silva, Marina I., et al.
Publicado: (2020)

Plasma Membrane Pores Drive Inflammatory Cell Death
por: Kolbrink, Benedikt, et al.
Publicado: (2020)

Contribution of large-pore channels to inflammation induced by microorganisms
por: Vega, José L., et al.
Publicado: (2023)

Activation of α7-nAChRs Promotes the Clearance of α-Synuclein and Protects Against Apoptotic Cell Death Induced by Exogenous α-Synuclein Fibrils
por: Zhao, Jifeng, et al.
Publicado: (2021)

Complexin and Ca(2+) stimulate SNARE-mediated membrane fusion
por: Yoon, Tae-Young, et al.
Publicado: (2008)

Collagen IV-β1-Integrin Influences INS-1 Cell Insulin Secretion via Enhanced SNARE Protein Expression
por: Barillaro, Malina, et al.
Publicado: (2022)

Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association
por: Jiao, Junyi, et al.
Publicado: (2018)

GBA-Associated Synucleinopathies: Prime Candidates for Alpha-Synuclein Targeting Compounds
por: Brockmann, Kathrin
Publicado: (2020)

Parkinson’s Disease: A Nanotheranostic Approach Targeting Alpha-Synuclein Aggregation
por: Zoey, Fong LaiGuan, et al.
Publicado: (2021)

Synuclein Regulates Synaptic Vesicle Clustering and Docking at a Vertebrate Synapse
por: Fouke, Kaitlyn E., et al.
Publicado: (2021)

Cannot write session to /tmp/vufind_sessions/sess_cj0nhqf81u4u3hph0jdb31ea52