Results 31 to 40 of about 3,191 (253)

The SNAREs vti1a and vti1b have distinct localization and SNARE complex partners [PDF]

open access: yesEuropean 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

A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells [PDF]

open access: yes, 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   +5 more
core   +1 more source

Lateral Fluid Percussion Injury Impairs Hippocampal Synaptic Soluble N-Ethylmaleimide Sensitive Factor Attachment Protein Receptor Complex Formation

open access: yesFrontiers in Neurology, 2017
Traumatic brain injury (TBI) and the activation of secondary injury mechanisms have been linked to impaired cognitive function, which, as observed in TBI patients and animal models, can persist for months and years following the initial injury ...
Shaun W. Carlson   +5 more
doaj   +1 more source

Munc18-1 induces conformational changes of syntaxin-1 in multiple intermediates for SNARE assembly

open access: yesScientific Reports, 2020
In neuronal exocytosis, SNARE assembly into a stable four-helix bundle drives membrane fusion. Previous studies have revealed that the SM protein Munc18-1 plays a critical role for precise SNARE assembly with the help of Munc13-1, but the underlying ...
Sanghwa Lee   +7 more
doaj   +1 more source

SNARE complex in axonal guidance and neuroregeneration

open access: yesNeural Regeneration Research, 2018
Through complex mechanisms that guide axons to the appropriate routes towards their targets, axonal growth and guidance lead to neuronal system formation. These mechanisms establish the synaptic circuitry necessary for the optimal performance of the nervous system in all organisms. Damage to these networks can be repaired by neuroregenerative processes
Ulloa, Fausto   +4 more
openaire   +3 more sources

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat [PDF]

open access: yes, 2002
In eukaryotic cells, secretion is achieved by vesicular transport. Fusion of such vesicles with the correct target compartment relies on SNARE proteins on both vesicle (v-SNARE) and the target membranes (t-SNARE).
Rein, U.   +15 more
core   +1 more source

α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle

open access: yesCell Reports, 2016
Intracellular membrane fusion is mediated by dynamic assembly and disassembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs). α-SNAP guides NSF to disassemble SNARE complexes after membrane fusion.
Lu Ma   +7 more
doaj   +1 more source

Analysis of SEC9 suppression reveals a relationship of SNARE function to cell physiology. [PDF]

open access: yesPLoS ONE, 2009
BACKGROUND:Growth and division of Saccharomyces cerevisiae is dependent on the action of SNARE proteins that are required for membrane fusion. SNAREs are regulated, through a poorly understood mechanism, to ensure membrane fusion at the correct time and ...
Daniel C Williams, Peter J Novick
doaj   +1 more source

Munc 18-1 Protein Molecules Move between Membrane Molecular Depots Distinct from Vesicle Docking Sites [PDF]

open access: yes, 2013
Four evolutionarily conserved proteins are required for mammalian regulated exocytosis: three SNARE proteins, syntaxin, SNAP-25, and synaptobrevin, and the SM protein, Munc18-1. Here, using single-molecule imaging, we measured the spatial distribution of
Rickman, Colin   +9 more
core   +1 more source

An electrostatically preferred lateral orientation of SNARE complex suggests novel mechanisms for driving membrane fusion. [PDF]

open access: yesPLoS ONE, 2010
Biological membrane fusion is a basic cellular process catalyzed by SNARE proteins and additional auxiliary factors. Yet, the critical mechanistic details of SNARE-catalyzed membrane fusion are poorly understood, especially during rapid synaptic ...
Ting Guo, Lin-Chen Gong, Sen-Fang Sui
doaj   +1 more source

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