Cargando…

Multiple factors maintain assembled trans-SNARE complexes in the presence of NSF and αSNAP

Neurotransmitter release requires formation of trans-SNARE complexes between the synaptic vesicle and plasma membranes, which likely underlies synaptic vesicle priming to a release-ready state. It is unknown whether Munc18-1, Munc13-1, complexin-1 and synaptotagmin-1 are important for priming becaus...

Descripción completa

Detalles Bibliográficos
Autores principales:	Prinslow, Eric A, Stepien, Karolina P, Pan, Yun-Zu, Xu, Junjie, Rizo, Josep
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	eLife Sciences Publications, Ltd 2019
Materias:	Cell Biology
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6353594/ https://www.ncbi.nlm.nih.gov/pubmed/30657450 http://dx.doi.org/10.7554/eLife.38880

Ejemplares similares

Munc18-1 is crucial to overcome the inhibition of synaptic vesicle fusion by αSNAP
por: Stepien, Karolina P., et al.
Publicado: (2019)

An essential and NSF independent role for α-SNAP in store-operated calcium entry
por: Miao, Yong, et al.
Publicado: (2013)

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)

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)

Reconciling isothermal titration calorimetry analyses of interactions between complexin and truncated SNARE complexes
por: Prinslow, Eric A, et al.
Publicado: (2017)

Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP
por: Weber, Thomas, et al.
Publicado: (2000)

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

SNARE assembly enlightened by cryo-EM structures of a synaptobrevin–Munc18-1–syntaxin-1 complex
por: Stepien, Karolina P., et al.
Publicado: (2022)

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

The linker domain of the SNARE protein SNAP25 acts as a flexible molecular spacer that ensures efficient S-acylation
por: Salaun, Christine, et al.
Publicado: (2020)

Fusion of tethered membranes can be driven by Sec18/NSF and Sec17/αSNAP without HOPS
por: Song, Hongki, et al.
Publicado: (2021)

The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions
por: Mertins, Jasmin, et al.
Publicado: (2021)

ER assembly of SNARE complexes mediating formation of partitioning membrane in Arabidopsis cytokinesis
por: Karnahl, Matthias, et al.
Publicado: (2017)

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

The Uso1 globular head interacts with SNAREs to maintain viability even in the absence of the coiled-coil domain
por: Bravo-Plaza, Ignacio, et al.
Publicado: (2023)

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)

Sec17 (α-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo
por: Schwartz, Matthew L, et al.
Publicado: (2017)

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

HOPS recognizes each SNARE, assembling ternary trans-complexes for rapid fusion upon engagement with the 4th SNARE
por: Song, Hongki, et al.
Publicado: (2020)

Membrane Binding of α-Synuclein Stimulates Expansion of SNARE-Dependent Fusion Pore
por: Khounlo, Ryan, et al.
Publicado: (2021)

Ubiquitination drives COPI priming and Golgi SNARE localization
por: Date, Swapneeta S, et al.
Publicado: (2022)

Epigallocatechin gallate inhibits SNARE‐dependent membrane fusion by blocking trans‐SNARE assembly
por: Zhu, Min, et al.
Publicado: (2022)

The SNAP-25 linker supports fusion intermediates by local lipid interactions
por: Shaaban, Ahmed, et al.
Publicado: (2019)

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

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)

Auxin regulates SNARE-dependent vacuolar morphology restricting cell size
por: Löfke, Christian, et al.
Publicado: (2015)

A ribosome assembly stress response regulates transcription to maintain proteome homeostasis
por: Albert, Benjamin, et al.
Publicado: (2019)

Analysis of asymmetry in lipid and content mixing assays with reconstituted proteoliposomes containing the neuronal SNAREs
por: Pan, Yun-Zu, et al.
Publicado: (2020)

Molecular machinery turns full circle
por: Rizo, Josep, et al.
Publicado: (2021)

COPI mediates recycling of an exocytic SNARE by recognition of a ubiquitin sorting signal
por: Xu, Peng, et al.
Publicado: (2017)

The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes
por: Zick, Michael, et al.
Publicado: (2013)

Rabphilin 3A binds the N-peptide of SNAP-25 to promote SNARE complex assembly in exocytosis
por: Li, Tianzhi, et al.
Publicado: (2022)

Expression of the SNARE Protein SNAP-23 Is Essential for Cell Survival
por: Kaul, Sunil, et al.
Publicado: (2015)

LAP2alpha maintains a mobile and low assembly state of A-type lamins in the nuclear interior
por: Naetar, Nana, et al.
Publicado: (2021)

The postsynaptic t-SNARE Syntaxin 4 controls traffic of Neuroligin 1 and Synaptotagmin 4 to regulate retrograde signaling
por: Harris, Kathryn P, et al.
Publicado: (2016)

Dynamic Binding Mode of a Synaptotagmin-1-SNARE Complex in Solution
por: Brewer, Kyle D., et al.
Publicado: (2015)

The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation
por: Eisemann, Travis J, et al.
Publicado: (2020)

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

Arrest of trans-SNARE zippering uncovers loosely and tightly docked intermediates in membrane fusion
por: Yavuz, Halenur, et al.
Publicado: (2018)

An essential step of kinetochore formation controlled by the SNARE protein Snap29
por: Morelli, Elena, et al.
Publicado: (2016)

Cannot write session to /tmp/vufind_sessions/sess_e3h49q6bkquo7lug4h87qj06fl