scholarly journals The destructive effect of botulinum neurotoxins on the SNARE protein: SNAP-25 and synaptic membrane fusion

PeerJ ◽  
2015 ◽  
Vol 3 ◽  
pp. e1065 ◽  
Author(s):  
Bin Lu
Keyword(s):  
Membrane Fusion ◽  
Synaptic Membrane ◽  
Snare Protein ◽  
Destructive Effect ◽  
Botulinum Neurotoxins

scholarly journals Membrane fusion mediated by peptidic SNARE protein analogues: Evaluation of FRET‐based bulk leaflet mixing assays

2021 ◽  
Author(s):  
Barbara E. Hubrich ◽  
Jan‐Dirk Wehland ◽  
Mike C. Groth ◽  
Anastasiya Schirmacher ◽  
Raphael Hubrich ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Snare Protein

Syntaxin Clustering and Optogenetic Control for Synaptic Membrane Fusion

2020 ◽  
Vol 432 (17) ◽  
pp. 4773-4782 ◽  
Author(s):  
Miaoling Li ◽  
Teak-Jung Oh ◽  
Huaxun Fan ◽  
Jiajie Diao ◽  
Kai Zhang
Keyword(s):  
Membrane Fusion ◽  
Synaptic Membrane ◽  
Optogenetic Control

scholarly journals Diverse Role of SNARE Protein Sec22 in Vesicle Trafficking, Membrane Fusion, and Autophagy

Cells ◽  
2019 ◽  
Vol 8 (4) ◽  
pp. 337 ◽  
Author(s):  
Muhammad Adnan ◽  
Waqar Islam ◽  
Jing Zhang ◽  
Wenhui Zheng ◽  
Guo-Dong Lu
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
Protein Secretion ◽  
Plasma Membranes ◽  
Extracellular Enzymes ◽  
Vesicle Trafficking ◽  
Cellular Systems ◽  
Rnai Pathway ◽  
Snare Protein ◽  
Genetic Redundancy

Protein synthesis begins at free ribosomes or ribosomes attached with the endoplasmic reticulum (ER). Newly synthesized proteins are transported to the plasma membrane for secretion through conventional or unconventional pathways. In conventional protein secretion, proteins are transported from the ER lumen to Golgi lumen and through various other compartments to be secreted at the plasma membrane, while unconventional protein secretion bypasses the Golgi apparatus. Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) proteins are involved in cargo vesicle trafficking and membrane fusion. The ER localized vesicle associated SNARE (v-SNARE) protein Sec22 plays a major role during anterograde and retrograde transport by promoting efficient membrane fusion and assisting in the assembly of higher order complexes by homodimer formation. Sec22 is not only confined to ER–Golgi intermediate compartments (ERGIC) but also facilitates formation of contact sites between ER and plasma membranes. Sec22 mutation is responsible for the development of atherosclerosis and symptoms in the brain in Alzheimer’s disease and aging in humans. In the fruit fly Drosophila melanogaster, Sec22 is essential for photoreceptor morphogenesis, the wingless signaling pathway, and normal ER, Golgi, and endosome morphology. In the plant Arabidopsis thaliana, it is involved in development, and in the nematode Caenorhabditis elegans, it is in involved in the RNA interference (RNAi) pathway. In filamentous fungi, it affects cell wall integrity, growth, reproduction, pathogenicity, regulation of reactive oxygen species (ROS), expression of extracellular enzymes, and transcriptional regulation of many development related genes. This review provides a detailed account of Sec22 function, summarizes its domain structure, discusses its genetic redundancy with Ykt6, discusses what is known about its localization to discrete membranes, its contributions in conventional and unconventional autophagy, and a variety of other roles across different cellular systems ranging from higher to lower eukaryotes, and highlights some of the surprises that have originated from research on Sec22.

Corrigendum to “Syntaxin Clustering and Optogenetic Control for Synaptic Membrane Fusion” [J. Mol. Biol. 432 (2020) 4773–4782]

2020 ◽  
Vol 432 (23) ◽  
pp. 6228-6229
Author(s):  
Miaoling Li ◽  
Teak-Jung Oh ◽  
Huaxun Fan ◽  
Jiajie Diao ◽  
Kai Zhang
Keyword(s):  
Membrane Fusion ◽  
Synaptic Membrane ◽  
Optogenetic Control

Differential Regulation of α-Granule and Dense Granule Secretion by an Actin Cytoskeletal Barrier.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 3528-3528
Author(s):  
Robert Flaumenhaft ◽  
James R. Dilks ◽  
Nataliya Rozenvayn ◽  
Rita A. Monahan-Earley ◽  
Dian Feng ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Actin Polymerization ◽  
Dense Granule ◽  
Snare Protein ◽  
Latrunculin A ◽  
Cytochalasin E ◽  
Dense Granule Secretion ◽  
Granule Secretion ◽  
Cytoskeletal Disruption ◽  
Granule Release

Abstract Platelet granule secretion is an essential component of normal arterial thrombus formation. Stimulation of platelets with strong agonists results in centralization of cytoplasmic organelles and loss of granules. These observations have lead to the supposition that cytoskeletal contraction facilitates granule secretion. Yet, the influence of the actin cytoskeleton in controlling membrane fusion events required for granule secretion remains largely unknown. Initial studies using electron microscopy revealed that the actin disrupting agents latrunculin A (4 μM) or cytochalasin E (4 μM) prevented pseudopod formation and granule centralization in platelets exposed to SFLLRN or PMA, but did not prevent degranulation. We next determined the effects of disruption of the actin cytoskeleton on α-granule secretion by monitoring P-selectin expression and β-thromboglobulin release. Incubation of platelets with either latrunculin A or cytochalasin E failed to stimulate α-granule secretion, but increased the rate of SFLLRN-induced α-granule secretion by 3.5-fold. Cytoskeletal disruption also augmented the degree of SFLLRN-induced α-granule secretion by 41±18% and reduced the amount of SFLLRN required to cause half-maximal stimulation by 2-fold. Incubation with latrunculin A stimulated α-granule secretion by the weak secretogues epinephrine or ADP by 7.6-fold and 5.4-fold, respectively. Cytoskeletal disruption also facilitated β-thromboglobulin release in response to SFLLRN, epinephrine, or ADP. In platelets permeabilized in the absence of ATP, exposure to 2 μM latrunculin A resulted in a 6.5- and 3.5-fold increase in α-granule release induced by Ca2+- or GTP-γ-S, respectively. Antibodies directed at a SNARE protein termed vesicle-associated fusion protein (VAMP) inhibited latrunculin A-dependent α-granule secretion. Thus, disruption of the actin cytoskeletal barrier by latrunculin A supports SNARE protein-dependent membrane fusion. Since actin acts as a barrier to α-granule secretion, we evaluated α-granules purified by subcellular fractionation for the presence of F-actin. Purified α-granules, but not phospholipid micelles, bound the F-actin probe FITC-phalloidin as determined by flow cytometry. FITC-phalloidin binding was inhibited in a dose-dependent manner by latrunculin A. These data indicated that α-granules are coated with F-actin that could serve a barrier function. We next evaluated the effects of cytoskeletal disruption on dense granule secretion by monitoring ADP/ATP release using a luciferin-luciferase based assay and by quantifying [3H]serotonin release. Cytoskeletal disruption by 4 μM latrunculin A failed to affect the degree of dense granule secretion from platelets stimulated by either SFLLRN, epinephrine, or ADP. Yet, 200 μM latrunculin A stimulated substantial dense granule release in the absence of agonist exposure and augmented SFLLRN-induced dense granule release by 2-fold. In contrast, 200 μM latrunculin A abolished SFLLRN-induced α-granule secretion. These observations indicate that the cytoskeleton differentially regulates α-granule and dense granule secretion. Our results also suggest that while some degree of actin polymerization is required for α-granule secretion, dense granule secretion is not dependent on actin polymerization.

scholarly journals α-SNAP Interferes with the Zippering of the SNARE Protein Membrane Fusion Machinery

2014 ◽  
Vol 289 (23) ◽  
pp. 16326-16335 ◽  
Author(s):  
Yongsoo Park ◽  
Wensi Vennekate ◽  
Halenur Yavuz ◽  
Julia Preobraschenski ◽  
Javier M. Hernandez ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Snare Protein ◽  
Protein Membrane

SNARE protein analog-mediated membrane fusion

2015 ◽  
Vol 21 (8) ◽  
pp. 621-629 ◽  
Author(s):  
Pawan Kumar ◽  
Samit Guha ◽  
Ulf Diederichsen
Keyword(s):  
Membrane Fusion ◽  
Snare Protein

scholarly journals Molecular Identification of a SNAP-25-Like SNARE Protein in Paramecium

2008 ◽  
Vol 7 (8) ◽  
pp. 1387-1402 ◽  
Author(s):  
Christina Schilde ◽  
Kaya Lutter ◽  
Roland Kissmehl ◽  
Helmut Plattner
Keyword(s):  
Fluorescent Protein ◽  
Heptad Repeat ◽  
Paramecium Tetraurelia ◽  
Snare Protein ◽  
Membrane Structures ◽  
Fusion Construct ◽  
Genome Duplications ◽  
Botulinum Neurotoxins ◽  
Food Vacuoles ◽  
Green Fluorescent

ABSTRACT Using database searches of the completed Paramecium tetraurelia macronuclear genome with the metazoan SNAP-25 homologues, we identified a single 21-kDa Qb/c-SNARE in this ciliated protozoan, named P. tetraurelia SNAP (PtSNAP), containing the characteristic dual heptad repeat SNARE motifs of SNAP-25. The presence of only a single Qb/c class SNARE in P. tetraurelia is surprising in view of the multiple genome duplications and the high number of SNAREs found in other classes of this organism. As inferred from the subcellular localization of a green fluorescent protein (GFP) fusion construct, the protein is localized on a variety of intracellular membranes, and there is a large soluble pool of PtSNAP. Similarly, the PtSNAP that is detected with a specific antibody in fixed cells is associated with a number of intracellular membrane structures, including food vacuoles, the contractile vacuole system, and the sites of constitutive endo- and exocytosis. Surprisingly, using gene silencing, we could not assign a role to PtSNAP in the stimulated exocytosis of dense core vesicles (trichocysts), but we found an increased number of food vacuoles in PtSNAP-silenced cells. In conclusion, we identify PtSNAP as a Paramecium homologue of metazoan SNAP-25 that shows several divergent features, like resistance to cleavage by botulinum neurotoxins.

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