The cytoplasmic domain of synaptobrevin contains a signal for localization to the synapse. Addition of synaptobrevin amino acids 1-93 onto the NH2-terminus of the transferrin receptor, which is normally excluded from the axon, was sufficient to direct this chimera to presynaptic sites where it colocalized with the synaptic vesicle protein synaptophysin. Localization of the chimera to the synapse was not due to inactivation of the dendritic targeting signal in the transferrin receptor, because a mutated transferrin receptor lacking the dendritic targeting motif but without added synaptobrevin sequences entered the axon but did not accumulate at synapses (West et al., 1997). This observation suggests that synapse targeting is a separate event from axonal entry. The synapse-targeting signal was not restricted to a single, 10-amino acid region of synaptobrevin, which indicates that the signal is either (a) redundant, (b) not colinear, or (c) dependent on the global conformation of the molecule. ...
The synaptic vesicle protein synaptobrevin (VAMP) has recently been implicated as one of the key proteins involved in exocytotic membrane fusion. It interacts with the synaptic membrane proteins syntaxin I and synaptosome-associated protein (SNAP)-25 to form a complex which precedes exocytosis [Söll …
Research proven purified goat polyclonal VAMP-1 antibody. Involved in neurotransmission including synapse vesicle transport and release. VAMPs also appear to be significantly lowered in Alzheimers Disease. Designed for immunohistochemistry, western blotting, Direct ELISA and related applications. IHC and WB images in product description.
Ti-VAMP antibody (158.2) | | Vesicle-associated membrane protein 7 (VAMP-7), Synaptobrevin-like protein 1, Tetanus-insensitive VAMP (Ti-VAMP), SYBL1
Opens the Highlight Feature Bar and highlights feature annotations from the FEATURES table of the record. The Highlight Feature Bar can be used to navigate to and highlight other features and provides links to display the highlighted region separately. Links in the FEATURES table will also highlight the corresponding region of the sequence. More... ...
Involved in the targeting and/or fusion of transport vesicles to their target membrane. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.
Fusion of neurosecretory vesicles with the plasma membrane is mediated by SNARE proteins, which transfer a force to the membranes. However, the mechanism by which this force transfer induces fusion pore formation is still unknown. The neuronal vesicular SNARE protein synaptobrevin 2 (syb2) is anchored in the vesicle membrane by a single C-terminal transmembrane (TM) helix. In coarse-grain molecular-dynamics simulations, self-assembly of the membrane occurred with the syb2 TM domain inserted, as expected from experimental data. The free-energy profile for the position of the syb2 membrane anchor in the membrane was determined using umbrella sampling. To predict the free-energy landscapes for a reaction pathway pulling syb2 toward the extravesicular side of the membrane, which is the direction of the force transfer from the SNARE complex, harmonic potentials were applied to the peptide in its unbiased position, pulling it toward new biased equilibrium positions. Application of piconewton forces to the
VAMP2 - VAMP2 (untagged)-Human vesicle-associated membrane protein 2 (synaptobrevin 2) (VAMP2) available for purchase from OriGene - Your Gene Company.
Vamp4 - Vamp4 (untagged) - Mouse vesicle-associated membrane protein 4 (Vamp4), (10ug) available for purchase from OriGene - Your Gene Company.
The ERS-2 mission is very flexible, allowing changes in the acquisition planning with very short notice, which is a feature very much appreciated by EDISOFT, and especially by the users of our service. In addition, during the EDISOFT service it was possible to provide a vessel detection service in less than 1 hour after acquisition, which is the Sentinel 1 required timeliness.". Celestino Gómez Cid of GMV said: "The use of ERS-2 data has been the key to succeeding in the delivery of Maritime security-based services for national and European Union authorities. In particular, ERS-2 has provided the required products with less than a one-hour delay after acquisition and provided a near real time processing chain by downloading data close to the area of interest thanks to ground stations. "With its flexible and light product formats, ERS-2 has also simplified the processing and reduced the delays in transferring the data. In addition, it has matched the quality requirements for maritime security ...
TY - JOUR. T1 - Tracking SNARE complex formation in live endocrine cells. AU - An, Seong J.. AU - Almers, Wolfhard. PY - 2004/11/5. Y1 - 2004/11/5. N2 - Syntaxin, synaptosome-associated protein of 25 kD (SNAP25), and vesicle-associated membrane protein/synaptobrevin are collectively called SNAP receptor (SNARE) proteins, and they catalyze neuronal exocytosis by forming a "core complex." The steps in core complex formation are unknown. Here, we monitored SNARE complex formation in vivo with the use of a fluorescent version of SNAP25. In PC12 cells, we found evidence for a syntaxin-SNAP25 complex that formed with high affinity, required only the amino-terminal SNARE motif of SNAP25, tolerated a mutation that blocks formation of other syntaxin-SNAP25 complexes, and assembled reversibly when Ca2+ entered cells during depolarization. The complex may represent a precursor to the core complex formed during a Ca2+-dependent priming step of exocytosis.. AB - Syntaxin, synaptosome-associated protein of 25 ...
Acute insulin stimulation of glucose transport in fat and skeletal muscle occurs principally as a result of the hormonal induced translocation of the GLUT4 glucose transporter from intracellular vesicular stores to the plasma membrane. The precise mechanisms governing the fusion of GLUT4 vesicles with the plasma membrane are very poorly understood at present but may share some similarities with synaptic vesicle fusion, as vesicle-associated membrane protein (VAMP) and cellubrevin, two proteins implicated in the process of membrane fusion, are resident in GLUT4-containing vesicles isolated from rat and murine 3T3-L1 adipocytes respectively. In this study we show that proteolysis of both cellubrevin and VAMP, induced by electroporation of isolated rat adipocytes with tetanus toxin, does not impair insulin-stimulated glucose transport or GLUT4 translocation. The hormone was found to stimulate glucose uptake by approx. 16-fold in freshly isolated rat adipocytes. After a single electroporating pulse, ...
In this study, we demonstrated that tomosyn regulates the oligomerization of the SNARE complex and inhibits SNARE-dependent neurotransmitter release. We reconstituted tomosyn-induced oligomerization of the SNARE complex in vitro and showed that the WD-40 repeat domain of tomosyn has an intrinsic ability to catalyze the oligomerization of the SNARE complex. It was previously reported that the C-terminal VLD of tomosyn acts as a SNARE domain competing with VAMP-2 and thereby inhibiting the formation of the SNARE complex (Yokoyama et al., 1999; Pobbati et al., 2004). Consistent with these studies, our in vitro assay showed that the C-terminal VLD of tomosyn inhibits the formation of the SNARE complex. Therefore, we concluded that tomosyn potently inhibits SNARE-dependent synaptic vesicle fusion via both N-terminal WD-40 repeat domain-catalyzed oligomerization of the SNARE complex and C-terminal VLD-based competitive inhibition of SNARE complex formation.. Synaptic efficacy at mossy fiber synapses ...
Die integralen Vesikelmembranproteine Synaptophysin und Synaptobrevin interagieren in adulten Neuronen. Zusätzlich bildet Synaptobrevin mit den Plasmamembranproteinen Syntaxin und synaptosome-associated protein 25kDa (SNAP25) den SNAP-Rezeptor (SNARE)-Proteinkomplex, der Voraussetzung für die Fusion zwischen synaptischen Vesikeln und präsynaptischer Membran ist. Mit Synaptophysin interagierendes Synaptobrevin bindet jedoch nicht an den SNARE-Proteinen. Es wird daher vermutet, dass der Synaptophysin/Synaptobrevin-Komplex eine Art Reservepool für Synaptobrevin bei erhöhter neuronaler Aktivität darstellt und die Verfügbarkeit von Synaptobrevin während der Exozytose reguliert. Mit verschiedenen Ansätzen wurde versucht, den auf dem Vesikel befindlichen Komplex genauer zu charakterisieren und in seiner Funktion näher zu beschreiben. Nach Stimulation mit exozytosevermittelnden Substanzen dissoziierte der Synaptophysin/ Synaptobrevin-Komplex, sowohl unter nativen Bedingungen als auch bei ...
Timmers KI, Clark AE, Omatsu-Kanbe M, Whiteheart SW, Bennett MK, Holman GD and Cushman SW. Experimental Diabetes, Metabolism and Nutrition Section, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.. The vesicle-associated membrane proteins [VAMPs; vesicle SNAP receptors (v-SNAREs)] present on GLUT4-enriched vesicles prepared from rat adipose cells [Cain, Trimble and Lienhard (1992) J. Biol. Chem. 267, 11681-11684] have been identified as synaptobrevin 2 (VAMP 2) and cellubrevin (VAMP 3) by using isoform-specific antisera. Additional antisera identify syntaxins 2 and 4 as the predominant target membrane SNAP receptors (t-SNAREs) in the plasma membranes (PM), with syntaxin 3 at one-twentieth the level. Syntaxins 2 and 4 are enriched 5-10-fold in PM compared with low-density microsomes (LDM). Insulin treatment results in an 11-fold increase in immunodetectable GLUT4 in PM and smaller (approx. 2-fold) increases in VAMP 2 and ...
Role of the synaptobrevin C terminus in fusion pore formation.: Neurotransmitter release is mediated by the SNARE proteins synaptobrevin II (sybII, also known a
As eluded earlier, membrane fusion is mediated via a specialized set of proteins in the secretory vesicles and the plasma membrane. Three soluble N-ethylmaleimide- sensitive factor (NSF)-attachment protein receptors (SNAREs) have been implicated in membrane fusion [10]. Target membrane proteins, SNAP-25 and syntaxin (t-SNARE) and secretory vesicle-associated membrane protein (v-SNARE), are part of the conserved protein complex involved in fusion of opposing bilayers [9, 10]. Although the structure of SNARE complex formed by interacting native [19] or recombinant [20, 21] t- and v- SNAREs was known from studies using electron microscopy [19, 20] and x-ray crystallography [21], the molecular mechanism of the involvement of SNAREs to bring about membrane fusion remained unknown until two years ago [12]. To determine the molecular mechanism of SNARE-induced membrane fusion, the structure and arrangement of SNAREs associated with lipid bilayers were examined using atomic force microscopy. The bilayer ...
Phagocytosis depends on expansion of plasmalemmal pseudopods generated by focal actin delivery and polymerisation of membranes from intracellular swimming pools. phagocytosed latex beads. It really is noteworthy that, though it was essential for the internalisation of opsonised contaminants via FcR and CR, TI-VAMP was dispensable Indirubin for uptake of zymosan, which depends on many receptors including CR3, mannose receptors and Dectin1 (Herre which process can be of physiological relevance during plasma Indirubin membrane restoration in non-secretory cells such as for example endothelial cells and fibroblasts (Andrews, 2002; Griffiths and Blott, 2002). With this framework, the exocytosis of lysosomal vesicles, which can be triggered by calcium mineral and controlled by synaptotagmin VII (SytVII), has been proven to involve TI-VAMP/VAMP7 (Rao as well as the kinetics was began by incubating the plates at 37C, 7% CO2. At different period factors, the cells had been placed on snow, cleaned once ...
The protein encoded by this gene is a type IV membrane protein found in plasma and intracellular vesicle membranes. The encoded protein is found as a homodimer and as a heterodimer with VAPA. This protein also can interact with VAMP1 and VAMP2 and may be involved in vesicle trafficking. [provided by RefSeq, Jul 2008 ...
Syntaxin-1, synaptobrevin/VAMP, and SNAP25 interact to form the SNARE complex, which is required for synaptic vesicle docking and fusion. The protein encoded by this gene is membrane-associated and inhibits SNARE complex formation by binding free syntaxin-1. Expression of this gene appears to be brain-specific. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Dec 2015 ...
Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation.
the problem in the statistics is that you dont see the amount of users by country...not easy to reach the 1st place when ...youre ALONE ...
How is Target-Soluble NSF (N-Ethylmaleimide-Sensitive Factor) Attachment Protein Receptor abbreviated? t-SNARE stands for Target-Soluble NSF (N-Ethylmaleimide-Sensitive Factor) Attachment Protein Receptor. t-SNARE is defined as Target-Soluble NSF (N-Ethylmaleimide-Sensitive Factor) Attachment Protein Receptor rarely.
TY - JOUR. T1 - The SNARE proteins SNAP25 and synaptobrevin are involved in endocytosis at hippocampal synapses. AU - Zhang, Zhen. AU - Wang, Dongsheng. AU - Sun, Tao. AU - Xu, Jianhua. AU - Chiang, Hsueh Cheng. AU - Shin, Wonchul. AU - Wu, Ling Gang. PY - 2013/5/22. Y1 - 2013/5/22. N2 - SNAP25, an essential component of the soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (SNARE) complex that mediates exocytosis, is not considered to play a role in endocytosis, which couples to exocytosis by retrieving a similar amount of exocytosed vesicles. By knocking down SNAP25 and imaging slow endocytosis at a conventional synapse, the rat cultured hippocampal synapse, we found that SNAP25 is involved in slow, clathrin-dependent endocytosis. With similar techniques, we found that not only SNAP25, but also synaptobrevin is involved in slow endocytosis. These results provide the first evidence showing the dual role of SNAP25 and synaptobrevin in both exocytosis and slow ...
Intrinsically disordered proteins (IDPs) and their conformational transitions play an important role in neurotransmitter release at the neuronal synapse. Here, the SNARE proteins are essential by forming the SNARE complex that drives vesicular membrane fusion. While it is widely accepted that the SNARE proteins are intrinsically disordered in their monomeric prefusion form, important mechanistic aspects of this prefusion conformation and its lipid interactions, before forming the SNARE complex, are not fully understood at the molecular level and remain controversial. Here, by a combination of NMR and fluorescence spectroscopy methods, we find that vesicular synaptobrevin-2 (syb-2) in its monomeric prefusion conformation shows high flexibility, characteristic for an IDP, but also a high dynamic range and increasing rigidity from the N to C terminus. The gradual increase in rigidity correlates with an increase in lipid binding affinity from the N to C terminus. It could also explain the increased ...
Soluble N-ethylmaleimide sensitive factor attachment protein receptors (SNAREs) are critical proteins in membrane fusion, in both regulated and constitutive vesicular traffic. In addition, proteins that interact with the SNAREs are thought to regulate fusion. Vesicle-associated membrane protein-2 (V …
Synaptobrevin interacts with synaptophysin in membranes of adult small synaptic vesicles and forms the synaptophysin/synaptobrevin complex. In contrast to the SNARE complex the synaptophysin/synaptobrevin complex only occurs in adult rat brain but is absent in embryonic brain. Changes in the binding properties of synaptophysin are probably induced by a factor of low molecular weight and correlate with posttranslational modifications of the protein. The synaptophysin/synaptobrevin complex plays an important role within the presynaptic terminal promoting synaptobrevin to bind its SNARE partners at the plasma membrane. In times of increased synaptic activity at the synapse the synaptophysin/synaptobrevin complex accelerates the recruitment of synaptobrevin to form new SNARE complexes and allows for fast exocytotic/endocytotic cycles. The synaptophysin/synaptobrevin complex and the SNARE complex are mutually exclusive. Major constituents of synaptic membranes are lipids and proteins which are ...
In summary, Ehlers and colleagues (Lee et al., 2010) use infection of a tetanus toxin light chain to silence isolated synapses and uncaging of glutamate at single spines to reveal priming of individual synapses for LTP. The authors show that the underlying molecular mechanism involves an increase in NMDA receptor number and a switch in NMDA receptor phenotype from NR2A-containing to NR2B-containing receptors. Alterations in postsynaptic NMDA receptors are associated with an increase in postsynaptic Ca2+ and increase in the NMDA component of the EPSC. These findings are significant in that they show for the first time that metaplasticity, once thought to be a process involving a global change in the biophysical properties of entire neural networks, can occur within a single synapse. Understanding how changes in NMDA receptor number and subtype alter the threshold for potentiation is likely to cast light on the molecular mechanisms involved in plasticity and priming in general and increase our ...
Purpose: : Neurodegeneration is a pathological feature of diabetic retinal neuropathy. One key element of neurodegeneration is a reduction in the number of synaptic connections between neurons. The aim of this study was to test the hypothesis that diabetes decreases the expression of specific synaptic and structural proteins in the rat retina. Methods: : Antibodies were used to detect synaptophysin, synapsin I, vesicle-associated membrane protein 2 (VAMP2), and postsynaptic density (PSD95), in retinas from three-month streptozotocin-diabetic and age-matched control male Sprague-Dawley rats, by western and immunohistochemistry with confocal microscopy. mRNA content for the same genes was quantified by RT-qPCR. ß-actin was used as an endogenous control in all assays. Results: : Diabetes significantly decreased synaptic, but not ß-actin, protein content detected by western blotting. RT-qPCR demonstrated similar significant decreases in mRNA transcript for these proteins. Synaptic protein ...
Vesicle-associated membrane protein-associated protein A is a protein that in humans is encoded by the VAPA gene. Together with VAPB it forms the VAP protein family. The protein encoded by this gene is a type IV membrane protein. It is present in the plasma membrane and intracellular vesicles. It may also be associated with the cytoskeleton. This protein may function in vesicle trafficking, membrane fusion, protein complex assembly and cell motility. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified. VAPA has been shown to interact with OSBP. This interaction is mediated by the FFAT motif in OSBP. GRCh38: Ensembl release 89: ENSG00000101558 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000024091 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Nishimura Y, Hayashi M, Inada H, Tanaka T (Feb 1999). "Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane ...
VAPA antibody for detecting human vesicle-associated membrane protein-associated protein A. Validated on up to 12 cell lysates for western blotting. Try a trial size today.
Rabbit Polyclonal Anti-VAMP3/Cellubrevin Antibody. Validated: WB, ICC/IF. Tested Reactivity: Human, Mouse, Rat, and more. 100% Guaranteed.
cis-SNARE complex (SNARE) -- are a large protein superfamily consisting of more than 60 members in yeast and mammalian cells. fact lexicon with terms going straight to the point. Facts are sorted by community importance and you can build your personalized lexicon
VAMP7 (also called tetanus-insensitive or TI-VAMP) may be the founding member of the ... deficient central synapses is not mediated by cellubrevin.
The Millicell-ERS-2 (Electrical Resistance System) voltohmmeter for cell analysis reliably measures membrane potential and resistance of epithelial cells in culture .
TY - JOUR. T1 - Munc18-1 binds directly to the neuronal SNARE complex. AU - Dulubova, Irina. AU - Khvotchev, Mikhail. AU - Liu, Siqi. AU - Huryeva, Iryna. AU - Südhof, Thomas C.. AU - Rizo-Rey, Jose. PY - 2007/2/20. Y1 - 2007/2/20. N2 - Both SM proteins (for Sec1/Munc18-like proteins) and SNARE proteins (for soluble NSF-attachment protein receptors) are essential for intracellular membrane fusion, but the general mechanism of coupling between their functions is unclear, in part because diverse SM protein/SNARE binding modes have been described. During synaptic vesicle exocytosis, the SM protein Munc18-1 is known to bind tightly to the SNARE protein syntaxin-1, but only when syntaxin-1 is in a closed conformation that is incompatible with SNARE complex formation. We now show that Munc18-1 also binds tightly to assembled SNARE complexes containing syntaxin-1. The newly discovered Munc18-1/SNARE complex interaction involves contacts of Munc18-1 with the N-terminal Habc domain of syntaxin-1 and the ...
TY - JOUR. T1 - Synaptic vesicle proteins and regulated exocytosis.. AU - Elferink, Lisa. AU - Scheller, R. H.. PY - 1993. Y1 - 1993. N2 - The recent identification of novel proteins associated with the membranes of synaptic vesicles has ignited the field of molecular neurobiology to probe the function of these molecules. Evidence is mounting that the vesicle proteins vamp (synaptobrevin), rab3A, synaptophysin, synaptotagmin (p65) and SV2 play an important role in regulated exocytosis, by regulating neurotransmitter uptake, vesicle targeting and fusion with the presynaptic plasma membrane.. AB - The recent identification of novel proteins associated with the membranes of synaptic vesicles has ignited the field of molecular neurobiology to probe the function of these molecules. Evidence is mounting that the vesicle proteins vamp (synaptobrevin), rab3A, synaptophysin, synaptotagmin (p65) and SV2 play an important role in regulated exocytosis, by regulating neurotransmitter uptake, vesicle ...
SNARE proteins participate in recognition and fusion of membranes. A SNARE complex consisting of vti1b, syntaxin 8, syntaxin 7, and endobrevin/VAMP-8 which is required for fusion of late endosomes in vitro has been identified recently. Here, we generated mice deficient in vti1b to study the function of this protein in vivo. vti1b-deficient mice had reduced amounts of syntaxin 8 due to degradation of the syntaxin 8 protein, while the amounts of syntaxin 7 and endobrevin did not change. These data indicate that vti1b is specifically required for the stability of a single SNARE partner. vti1b-deficient mice were viable and fertile. Most vti1b-deficient mice were indistinguishable from wild-type mice and did not display defects in transport to the lysosome. However, 20% of the vti1b-deficient mice were smaller. Lysosomal degradation of an endocytosed protein was slightly delayed in hepatocytes derived from these mice. Multivesicular bodies and autophagic vacuoles accumulated in hepatocytes of some ...
In support of this hypothesis, defects in SNARE complex assembly and traffic through the endosomal system due to the loss of Vps45p (Vps is vacuolar protein sorting) are bypassed by a version of the yeast endocytic Sx, Tlg2p, lacking its Habc domain [19]. These results support a model whereby Vps45p activates Tlg2p for entry into functional SNARE complexes by facilitating its switch from a closed to an open conformation. The version lacking the Habc domain is unable to adopt the closed conformation and therefore does not require activation (opening) by Vps45p. Although these functional studies indicate that, like the plasma membrane Sxs described above, Tlg2p adopts a closed conformation that is incompatible with SNARE complex formation, NMR spectroscopy studies have been used to argue that this endosomal Sx does not adopt a closed conformation [20]. However, the bacterially produced version of Tlg2p used in these studies lacked almost half of the SNARE motif. Through analogy with the closed ...
In rodents and humans, alcohol exposure has been shown to predispose the pancreas to cholinergic or viral induction of pancreatitis. We previously developed a rodent model in which exposure to an ethanol (EtOH) diet, followed by carbachol (Cch) stimulation, redirects exocytosis from the apical to the basolateral plasma membrane of acinar cells, resulting in ectopic zymogen enzyme activation and pancreatitis. This redirection of exocytosis involves a soluble NSF attachment receptor (SNARE) complex consisting of syntaxin-4 and synapse-associated protein of 23 kDa (SNAP-23). Here, we investigated the role of the zymogen granule (ZG) SNARE vesicle-associated membrane protein 8 (VAMP8) in mediating basolateral exocytosis. In WT mice, in vitro EtOH exposure or EtOH diet reduced Cch-stimulated amylase release by redirecting apical exocytosis to the basolateral membrane, leading to alcoholic pancreatitis. Further reduction of zymogen secretion, caused by blockade of both apical and basolateral ...
Vesicle associated membrane proteins are members of the soluble N-ethyl-maleimide-sensitive factor receptor (SNARE) attachment protein family that facilitate the intracellular membrane fusion process involved in neurotransmitter release (Ungar & Hughson, 2003). Cellubrevin, or VAMP-3, is similar to SNARE proteins, synaptobrevin 1 and 2 (VAMP-1 and 2), but can be found in many different tissues such as fibroblasts, adipose cells, insulin-secreting B cells, and supportive brain cells like glial, but not brain neuron cells (Chilcote et al., 1995). However cellubrevin is also a substrate for proteolytic action of tetanus toxin just like VAMP-1 and 2, and suggests similar roles in exocytosis due to the blocking of neurotransmitter release in the presence of tetanus (Chilcote et al., 1995). Cellubrevin has been found to be significant in the docking and vesicle fusion process of secretory granules to the plasma membrane, but few studies in the immunofluorescence localization on subcellular fractions ...
In eukaryotic cells, membrane-bound vesicles carry cargo between intracellular compartments, to and from the cell surface, and to the extracellular environment. Many conserved families of proteins are required for properly localized vesicle fusion, including the multi-subunit tethering complexes and the SNARE complexes. These protein complexes work together to promote proper vesicle fusion in other trafficking pathways. Contrary to these other pathways, our lab previously suggested that the exocyst subunit Sec6, a component of the exocytosis-specific tethering complex, inhibited Sec9:Sso1 SNARE complex assembly due to interactions in vitro with the SNARE protein Sec9 (Sivaram et al., 2005). My goal for this project was to test the hypothesis that Sec6 inhibited SNARE complex assembly in vivo. I therefore chose to generate Sec6:Sec9 loss-of-binding mutants, and study their effect both in vitro and in vivo. I identified a patch of residues on Sec9 that, when mutated, are sufficient to disrupt the novel
The vacuole system provides good tools to assay the abundance of the tagged SNAREs on the isolated organelle, dissect their molecular interactions, and to identify hemifusion intermediates. In contrast to previous studies on tagged synaptobrevin II in chromaffin cells, in which these molecular properties are hard to access [40], this allowed us to demonstrate that the effect of large luminal tags was restricted to content mixing, whereas lipid mixing was essentially unaffected. This suggests that mixing of the outer leaflets may be less dependent on a collective perturbation of lipid structure by SNARE TMDs than the rearrangement of the inner leaflets. It is consistent with theory and simulations on the energetics of SNARE‐driven fusion, which suggested that fusion pore opening is limited by a larger free energy barrier than the induction of hemifusion [38]. In line with this, opening of the fusion pore has been found to be rate‐limiting for vacuole fusion [22].. The observation that even ...
We next investigated whether MAPK activation by AMPA regulates key presynaptic effectors or the dynamics of synaptic vesicles. To this aim, we first focused on the synaptic vesicle-associated protein synapsin I, which is the major presynaptic substrate for MAPK (Jovanovic et al., 2000). In isolated growth cone particles, stimulation with AMPA specifically increased the Triton X-100 solubility of synapsin I, without affecting the Triton X-100 solubility of other synaptic vesicle proteins (Fig. 3A). This effect was mimicked by BDNF, a potent activator of MAPK, and was prevented by the MEK inhibitor PD98059 (Fig. 3B) and by GYKI52466 (data not shown). The increased recovery of synapsin I in the Triton X-100-soluble fraction occurred in parallel with MAPK activation and with the phosphorylation of synapsin I at MAPK-specific sites 4 and 5 (Fig. 3B). Thus, the increased Triton X-100 solubility of synapsin I could be a consequence of the MAPK-dependent phosphorylation.. Once it was defined that the ...
VAPB antibody for detecting human vesicle-associated membrane protein-associated protein B/C. Validated on up to 12 cell lysates for western blotting. Try a trial size today.
An intravascular snare device for use in capturing debris found in blood vessels. The snare device is fabricated from a tube and includes longitudinally and circumferentially extending members. The snare device specifically embodies structure that provides enhanced radial opening and angular resistance to collapse.
With 33% smaller snare wire, the Exacto cold snare offers greater control for placement and resection compared to other colonoscopy snares.
Snare Drum Size: 14 x 05, Multisonic series, MS514BD, Brass drum shell, 10 Tension rods, Strainer with 5 different snare wires, Die-cast hoops
Mso1p-Sec4p colocalization is depended on Sec2p and independent of a functional SNARE complex. (A) wt, (B) sso2-1 Δsso1, and (C) sec2-41 cells coexpressing
Kit Component:- KN202734G1, VAMP4 gRNA vector 1 in pCas-Guide vector- KN202734G2, VAMP4 gRNA vector 2 in pCas-Guide vector- KN202734D, donor vector…