Results 51 to 60 of about 73,344 (342)
A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells [PDF]
, 2008 Mannose 6-phosphate receptors (MPRs) are transported from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This process requires Rab9 guanosine triphosphatase (GTPase) and the putative tether GCC185.
Espinosa, Eric +2 more
core +4 more sources
The SNAREs vti1a and vti1b have distinct localization and SNARE complex partners [PDF]
European Journal of Cell Biology, 2002 Two mammalian proteins, vtila and vtilb, are homologous to the yeast Q-SNARE Vtilp which is part of several SNARE complexes in different transport steps. In vitro experiments suggest distinct functions for vtila and vtilb. Here we compared the subcellular localization of endogenous vtila and vtilb by immunofluorescence and immuno-electron microscopy ...
Kreykenbohm, V +4 more
openaire +5 more sources
The destructive effect of botulinum neurotoxins on the SNARE protein: SNAP-25 and synaptic membrane fusion [PDF]
PeerJ, 2015 Synaptic exocytosis requires the assembly of syntaxin 1A and SNAP-25 on the plasma membrane and synaptobrevin 2 (VAMP2) on the vesicular membrane to bridge the two opposite membranes.
Bin Lu
doaj +2 more sources
Frontiers in Molecular Neuroscience, 2017 The Ca2+ sensor synaptotagmin-1 (Syt1) plays an essential function in synaptic exocytosis. Recently, Syt1 has been implicated in synaptic vesicle priming, a maturation step prior to Ca2+-triggered membrane fusion that is believed to involve formation of ...
Yun Li +5 more
doaj +1 more source
Doc2b Protects β-Cells Against Inflammatory Damage and Enhances Function [PDF]
, 2018 Loss of functional β-cell mass is an early feature of type 1 diabetes. To release insulin, β-cells require soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes, as well as SNARE complex regulatory proteins like double ...
Ahn, Miwon +9 more
core +1 more source
A Dynamic t-SNARE Complex [PDF]
Structure, 2008 Syntaxin-1/SNAP-25 heterodimers with 1:1 stoichiometry likely play a key role in neurotransmitter release but they have been difficult to characterize. In this issue of Structure, Weninger et al. present a beautiful single molecule spectroscopy study showing the dynamic nature of these heterodimers and how they are influenced by other factors.
openaire +1 more source
Three-dimensional structure of the complexin/snare complex [PDF]
Acta Crystallographica Section A Foundations of Crystallography, 2002 During neurotransmitter release, the neuronal SNARE proteins synaptobrevin/VAMP, syntaxin, and SNAP-25 form a four-helix bundle, the SNARE complex, that pulls the synaptic vesicle and plasma membranes together possibly causing membrane fusion. Complexin binds tightly to the SNARE complex and is essential for efficient Ca(2+)-evoked neurotransmitter ...
Chen, Xiaocheng +6 more
openaire +3 more sources
eLife, 2016 Complexin regulates spontaneous and activates Ca2+-triggered neurotransmitter release, yet the molecular mechanisms are still unclear. Here we performed single molecule fluorescence resonance energy transfer experiments and uncovered two conformations of
Ucheor B Choi +4 more
doaj +1 more source
Ein Indikator der Reifung synaptischer Vesikel [PDF]
, 1999 Titlepage, Contents 1\. Introduction 1.1 Synaptic transmission and plasticity 1.2 Proteins involved in exocytotic membrane fusion > 1.2.1 Synaptobrevin > > 1.2.2 Syntaxin > > 1.2.3 SNAP 25 1.3 Characterisation of the assembled fusion complex 1 ...
Becher, Anja
core +1 more source
Multiple factors maintain assembled trans-SNARE complexes in the presence of NSF and αSNAP
eLife, 2019 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.
Eric A Prinslow +4 more
doaj +1 more source