The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation
eLife, 2020 Fusion of intracellular trafficking vesicles is mediated by the assembly of SNARE proteins into membrane-bridging complexes. SNARE-mediated membrane fusion requires Sec1/Munc18-family (SM) proteins, SNARE chaperones that can function as templates to ...
Travis J Eisemann +5 more
doaj +1 more source
An electrostatically preferred lateral orientation of SNARE complex suggests novel mechanisms for driving membrane fusion. [PDF]
PLoS 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
SNARE Zippering Is Suppressed by a Conformational Constraint that Is Removed by v-SNARE Splitting
Cell Reports, 2021 Summary: Intracellular vesicle fusion is catalyzed by soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). Vesicle-anchored v-SNAREs pair with target membrane-associated t-SNAREs to form trans-SNARE complexes, releasing free ...
Yinghui Liu +5 more
doaj +1 more source
SNARE-Ware: The Role of SNARE-Domain Proteins in Plant Biology [PDF]
Annual Review of Cell and Developmental Biology, 2007 In yeast and animal cells, members of the superfamily of N-ethylmaleimide-sensitive factor adaptor protein receptor (SNARE)-domain-containing proteins are key players in vesicle-associated membrane fusion events during transport processes between individual compartments of the endomembrane system, including exocytosis and endocytosis.
Lipka, V., Kwon, C., Panstruga, R.
openaire +3 more sources
Epileptic Phenotypes Associated With SNAREs and Related Synaptic Vesicle Exocytosis Machinery
Frontiers in Neurology, 2022 SNAREs (soluble N-ethylmaleimide sensitive factor attachment protein receptor) are an heterogeneous family of proteins that, together with their key regulators, are implicated in synaptic vesicle exocytosis and synaptic transmission. SNAREs represent the
Elisa Cali +3 more
doaj +1 more source
A SNARE protective pool antagonizes APOL1 renal toxicity in Drosophila nephrocytes
Cell & Bioscience, 2023 Background People of Sub-Saharan African ancestry are at higher risk of developing chronic kidney disease (CKD), attributed to the Apolipoprotein L1 (APOL1) gene risk alleles (RA) G1 and G2. The underlying mechanisms by which the APOL1-RA precipitate CKD
Jin-Gu Lee +6 more
doaj +1 more source
SNARE proteins in membrane trafficking [PDF]
Traffic, 2017 SNAREsare the core machinery mediating membrane fusion. In this review, we provide an update on the recent progress onSNAREsregulating membrane fusion events, especially the more detailed fusion processes dissected by well‐developed biophysical methods and in vitro single molecule analysis approaches.
Tuanlao, Wang +2 more
openaire +2 more sources
Secretory vesicles are preferentially targeted to areas of low molecular SNARE density [PDF]
, 2012 Intercellular communication is commonly mediated by the regulated fusion, or exocytosis, of vesicles with the cell surface. SNARE (soluble N-ethymaleimide sensitive factor attachment protein receptor) proteins are the catalytic core of the secretory ...
Weiping Lu (120665) +32 more
core +1 more source
The SNARE protein family of Leishmania major [PDF]
BMC Genomics, 2006 Abstract Background Leishmania major is a protozoan parasite with a highly polarised cell shape that depends upon endocytosis and exocytosis from a single area of the plasma membrane, the flagellar pocket.
Besteiro, S. +2 more
openaire +4 more sources
ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat [PDF]
, 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