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Topic: SNARE protein

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	BioMed Central \| Full text \| The SNARE protein family of Leishmania major
		Indeed, the SNARE motif involved in the formation of the helical bundle of the SNARE complex is conserved but bears unique features allowing the classification as Q- and R-, according to the residue present in the centre of the motif [10].
		Proteins of the SM family appear to function at different intracellular membrane compartments, have generally a high specificity for one SNARE protein and are thought to act as chaperone-like molecules [30].
		The N-terminal series of Habc helixes from syntaxin 1 is proposed to be able to bind the coiled-coil region of the SNARE motif to prevent the protein from interacting with unwanted partners during its trafficking to the plasma membrane [23,40].
	www.biomedcentral.com /1471-2164/7/250 (7395 words)

	Interactive Fly, Drosophila
		SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] proteins are essential for membrane fusion and are conserved from yeast to humans.
		Syntaxin is a cytoplasmically oriented plasma membrane protein and VAMP (vesicle-associated membrane protein; synaptobrevin) is a protein associated with the secretory vesicle membrane.
		The proteins that reach the inappropriate domain are rapidly removed by endocytosis, whereas those that reach the appropriate domain interact with submembranous cytoskeletal proteins, which stabilize them in the membrane and prevent their endocytosis (Sampo, 2003 and references therein).
	www.sdbonline.org /fly/neural/syntaxn2.htm (6235 words)

	[No title]
		Soluble N-ethylmaleimide attachment protein receptor (SNARE) proteins are a family of membrane-associated proteins characterised by an alpha-helical coiled-coil domain called the SNARE motif [1].
		SNAREs are localised to distinct membrane compartments of the secretory and endocytic trafficking pathways, and contribute to the specificity of intracellular membrane fusion processes.
		The SNARE motif represented in this entry is found in the N-terminal domains of certain syntaxin family members: syntaxin 1a, which is required for neurotransmitter release[2], syntaxin 6, which is found in endosomal transport vesicles [3], yeast Sso1p [4], and Vam3p, a yeast syntaxin essential for vacuolar fusion [5].
	www.ebi.ac.uk /interpro/IEntry?ac=IPR010989 (478 words)

	[No title]
		Syntaxins A and B are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane.
		Members of the syntaxin family [2, 3] have a size ranging from 30 Kd to 40 Kd; a C-terminal extremity which is highly hydrophobic and anchors the protein on the cytoplasmic surface of cellular membranes; a central, well conserved region SNARE motif, which seems to be in a coiled-coil conformation.
		SNARE motifs assemble into parallel four helix bundles stabilised by the burial of these hydrophobic helix faces in the bundle core [4].
	www.ebi.ac.uk /interpro/IEntry?ac=IPR006012 (408 words)

	SNARE
		PRESYNAPTIC PROTEINS, SYNAPTIC VESICLE DOCKING and MEMBRANE FUSION
		Proteins bind in parallel and form 4 helix bundle
		Proteins with C-terminal R-SNARE motif: Inhibit normal SNARE assembly and exocytosis
	www.neuro.wustl.edu /neuromuscular/pathol/snare.htm (959 words)

	Characterization of a Novel Yeast SNARE Protein Implicated in Golgi Retrograde Traffic -- Lupashin et al. 8 (12): 2659 ...
		Protein transport and membrane flow in eukaryotic cells is mediated by vesicles that bud from one membrane-bounded compartment
		protein of the Golgi apparatus and the prevacuolar compartment.
		Hay, J.C., Hirling, H., and Scheller, R.H. Mammalian vesicle trafficking proteins of the endoplasmic reticulum and Golgi apparatus.
	www.molbiolcell.org /cgi/content/full/8/12/2659 (8028 words)

	Calcium Can Disrupt the SNARE Protein Complex on Sea Urchin Egg Secretory Vesicles without Irreversibly Blocking Fusion ...
		Proteins from CV membranes were extracted with Triton X-114, then dissolved in SDS sample buffer, boiled, and analyzed by SDS-PAGE on 12% gels followed by immunoblotting (50 µg of total protein/lane).
		The blot was probed with polyclonal antibodies to VAMP2 and syntaxin 1A and a monoclonal antibody to SNAP-25, as indicated.
		To test for the presence of a SNARE protein complex, CV membrane proteins were solubilized in 1% Triton X-100 prior to immunoprecipitation with anti-VAMP or anti-syntaxin antibodies.
	www.jbc.org /cgi/content/full/273/50/33667 (6361 words)

	HHMI News: Botulism Toxin Ensnares Its Target
		The nerve cell proteins are called SNAREs, which are key components of the machinery that nerve cells use to fire bursts of neurotransmitter chemicals to trigger neighboring nerves or activate muscle cells.
		Neurotoxin proteases that act by cleaving SNARE proteins are highly specific for their targets - meaning that each toxin specifically recognizes and attacks one of three different neuronal SNARE proteins.
		The researchers determined the structure of the bound proteins using x-ray diffraction, a widely used analytical technique whereby beams of x-rays are directed through crystallized proteins.
	www.hhmi.org /news/brunger2.html (874 words)

	Yeast VSM1 Encodes a v-SNARE Binding Protein That May Act as a Negative Regulator of Constitutive Exocytosis -- ...
		In the left panel, 50-µg protein aliquots from the different fractions obtained from cells maintained at 26°C were electrophoresed; 25-µg aliquots of protein were used in the experiment shown in the middle panel.
		Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle.
		The Drosophila Ras2 and Rop gene pair: a dual homology with a yeast Ras-like gene and a suppressor of its loss-of-function phenotype.
	mcb.asm.org /cgi/content/full/19/6/4480 (8931 words)

	Molecular Foundation (Site not responding. Last check: 2007-11-01)
		SNARE proteins are characterized by containing a SNARE motif, homologous helical 70-residue sequence that falls in 4 types (R, Qa, Qb, and Qc).
		SNARE complex formation pulls synaptic vesicle and plasma membranes close together by creating an unstable intermediate but not opening fusion pore.
		So the binding to synaptophysin is thought to have similar role -inhibit binding to other SNARE proteins.
	www.stanford.edu /~xujing/VAMP.htm (466 words)

	A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking -- Ungermann et al. 97 (16): ...
		A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking -- Ungermann et al.
		A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking
		Proteins from the pellet fraction were analyzed by SDS/PAGE and immunoblot with antibodies to Vam7p, Vti1p, and Ypt7p.
	www.pnas.org /cgi/content/full/97/16/8889 (2555 words)

	Soluble NSF Attachment Protein Receptors (SNAREs) in RBL-2H3 Mast Cells: Functional Role of Syntaxin 4 in Exocytosis ...
		In sensitive proteins, the immunoreactivity is lost due to the proteolysis of epitope-containing fragments (aa 1–76 in VAMP2 and cellubrevin), which run out of the SDS gel.
		A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells.
		Cellubrevin is a resident protein of insulin-sensitive GLUT4 glucose transporter vesicles in 3T3–L1 adipocytes.
	www.jimmunol.org /cgi/content/full/164/11/5850 (5938 words)

	Pfam 18.0 : SNARE (Site not responding. Last check: 2007-11-01)
		The SNARE domain is thought to act as a protein-protein interaction module in the assembly of a SNARE protein complex [1].
		The Syntaxins are type-I transmembrane proteins that contain several regions with coiled-coil propensity in their cytosolic part, the SNARE motif.
		SNARE motifs assemble into parallel four helix bundles stabilised by the burial of these hydrophobic helix faces in the bundle core.
	pfam.wustl.edu /cgi-bin/getdesc?name=SNARE (303 words)

	YKT6P-IS-MULTIFUNCTIONAL-YEAST-R-SNARE-THAT-IS-REQUIRED-FOR-MULTIPLE-MEMBRANE-TRANSPORT-PATHWAYS-TO-THE-VACUOLE (Site not responding. Last check: 2007-11-01)
		Intracellular membrane fusion requires that membrane-bound soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins on both vesicle and target membranes form a highly specific complex necessary to bring the membranes close in space.
		One mutation produces an early Golgi block to secretion, and overexpression of the SNARE protein Sft1p suppresses the growth and secretion defects of this mutation.
		Defects are seen in carboxypeptidase Y sorting, alkaline phosphatase transport, and aminopeptidase I delivery, and in one mutant, overexpression of the SNARE protein Nyv1p suppresses the alkaline phosphatase transport defect.
	biblioteca.universia.net /html_bura/ficha/params/id/428042.html (524 words)

	A SNARE required for retrograde transport to the endoplasmic reticulum -- Burri et al. 100 (17): 9873 -- Proceedings of ...
		A SNARE required for retrograde transport to the endoplasmic reticulum -- Burri et al.
		The SNARE motif is boxed in gray and the transmembrane domain is in boldface type.
		Involvement of Syntaxin 18, an Endoplasmic Reticulum (ER)-localized SNARE Protein, in ER-mediated Phagocytosis
	www.pnas.org /cgi/content/full/100/17/9873 (3532 words)

	Asymmetric Requirements for a Rab GTPase and SNARE Proteins in Fusion of COPII Vesicles with Acceptor Membranes -- Cao ...
		have implicated the SNAREs Sec22p, Bet1p, Bos1p, Ykt6, and Sed5p
		Nichols, B.J., Pelham, H.R.B. SNAREs and membrane fusion in the Golgi apparatus.
		Zhang, T., Wong, S.H., Tang, B.L., Xu, Y., Peter, F., Subramaniam, V.N., Hong, W. The mammalian protein (rbet1) homologous to yeast Bet1p is primarily associated with the pre-Golgi intermediate compartment and is involved in vesicular transport from the endoplasmic reticulum to the Golgi apparatus.
	www.jcb.org /cgi/content/full/149/1/55 (7243 words)

	What is the role of SNARE proteins in membrane fusion? -- Duman and Forte 285 (2): C237 -- AJP - Cell Physiology
		SNARE complex formation may also exert a force on membrane lipids, causing them to transition into a fusion intermediate (for simplicity, not shown here).
		SNAREs have been shown to be fairly promiscuous in their interactions.
		SNARE proteins contribute to calcium cooperativity of synaptic transmission.
	ajpcell.physiology.org /cgi/content/full/285/2/C237 (7921 words)

	Interactive Fly, Drosophila
		Two proteins thus far identified are unique to the synapse: Synaptotagmin, a protein that senses Ca++ levels, and a Cysteine string protein.
		A pair of cognate proteins, capable of pairing membranes and fusing their bilayers appears to be the simplest possible means, and one utilized by cells, to link a mechanism for specifically pairing membranes to a mechanism for fusing their bilayer.
		These proteins are believed to be involved in the fusion of transport vesicles with their target membrane.
	www.sdbonline.org /fly/neural/syntaxn1.htm (5477 words)

	Increased expression of the SNARE accessory protein Munc18c in lipid-mediated insulin resistance -- Schlaepfer et al. ...
		A: Munc18c protein levels are increased in the gastrocnemius muscle of mice fed HF compared with LF.
		Genomic structure of MUNC18-1 protein, which is involved in docking and fusion of synaptic vesicles in brain.
		Free fatty acid-induced insulin resistance is associated with activation of protein kinase C theta and alterations in the insulin signaling cascade.
	www.jlr.org /cgi/content/full/44/6/1174 (4690 words)

	Abnormal Expression of Pancreatic Islet Exocytotic Soluble N-Ethylmaleimide-Sensitive Factor Attachment Protein ...
		Immunoblots comparing the expressions of SNARE proteins, nSec1, and actin of islets obtained from vehicle (V)-treated GK and Wistar islets.
		Immunoblots comparing expressions of SNARE proteins, nSec1, and actin in the brains (5 µg crude lysates) of GK and Wistar rats.
		Protein (5 µg) from each sample was loaded, and protein loading was confirmed by Coomassie staining of the gels.
	endo.endojournals.org /cgi/content/full/143/11/4218 (4825 words)

	Regulation of syntaxin1A-munc18 complex for SNARE pairing in HEK293 cells -- Gladycheva et al. 558 (3): 857 -- The ...
		munc18 and munc13, EGFP, ECFP or EcYFP fluorescent protein was
		Phosphorylation of Munc18 by protein kinase C regulates the kinetics of exocytosis.
		The unc-18 gene encodes a novel protein affecting the kinetics of acetylcholine metabolism in the nematode Caenorhabditis elegans.
	jp.physoc.org /cgi/content/full/558/3/857 (6362 words)

	The Arabidopsis Genome. An Abundance of Soluble N-Ethylmaleimide-Sensitive Factor Adaptor Protein Receptors -- ...
		B, Four SNARE helicies are required for vesicle fusion to occur (labeled the a-, b-, c-, and d- helices as described in Scales et al., 2000
		Note that although the closest homologs of AtSec1a, AtSec1b, and KEULE are the animal exocytic Sec1 proteins, the three Arabidopsis Sec1 proteins cluster as a somewhat separate group and may have evolved to play novel roles (such as cytokinesis in the case of KEULE).
		Bassham DC, Raikhel NV (1998) An Arabidopsis VPS45p homolog implicated in protein transport to the vacuole.
	www.plantphysiol.org /cgi/content/full/124/4/1558 (6617 words)

	Identification of Domains Required for Developmentally Regulated SNARE Function in Saccharomyces cerevisiae -- Neiman ...
		S-labeled Sec9p was mixed with the indicated GST fusion proteins and precipitated on glutathione agarose as described in
		The band present at the position of Sec9p in the vector lane (lane 1) and the PSSS lane (lane 11) is the protein produced by the sec9-4 allele present in the strain background.
		, 1994 A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles.
	www.genetics.org /cgi/content/full/155/4/1643 (7327 words)

	Single Molecule Mechanical Probing of the SNARE Protein Interactions -- Liu et al. 91 (2): 744 -- Biophysical Journal
		Single Molecule Mechanical Probing of the SNARE Protein Interactions -- Liu et al.
		Exocytotic release of neurotransmitters is mediated by the ternary
		of the SNARE complex, that Sx1A and Sb2 are zippered throughout
	www.biophysj.org /cgi/content/abstract/91/2/744 (223 words)

	Calcium Can Disrupt the SNARE Protein Complex on Sea Urchin Egg Secretory Vesicles without Irreversibly Blocking Fusion ...
		SNARE interactions are not needed at the time of fusion.
		A single amino acid near the C terminus of the synaptosomeassociated protein of 25 kDa (SNAP-25) is essential for exocytosis in chromaffin cells
		Activation of Annexin 7 by Protein Kinase C in Vitro and in Vivo
	www.jbc.org /cgi/content/abstract/273/50/33667 (1109 words)

	UniProtKB/Swiss-Prot entry O95295 [S25BP_HUMAN] SNARE-associated protein Snapin
		Starcevic M. Dell'Angelica E.C. "Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1).";
		Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis.
		View cluster of proteins with at least 50% / 90% / 100% identity.
	www.expasy.org /uniprot/O95295 (450 words)

	Characterization of a Novel Yeast SNARE Protein Implicated in Golgi Retrograde Traffic -- Lupashin et al. 8 (12): 2659 ...
		The SNARE Vti1a-beta Is Localized to Small Synaptic Vesicles and Participates in a Novel SNARE Complex
		Sec34p, a Protein Required for Vesicle Tethering to the Yeast Golgi Apparatus, Is in a Complex with Sec35p
		SGR2, a Phospholipase-Like Protein, and ZIG/SGR4, a SNARE, Are Involved in the Shoot Gravitropism of Arabidopsis
	www.molbiolcell.org /cgi/content/abstract/8/12/2659 (1655 words)

	UniProtKB/Swiss-Prot entry O15498 [YKT6_HUMAN] Synaptobrevin homolog YKT6
		Tai G. Lu L. Wang T.L. Tang B.L. Goud B. Johannes L. Hong W. "Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the trans-Golgi network.";
		Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5.
		Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5.
	ca.expasy.org /uniprot/O15498 (646 words)

	G protein
		This has been attributed in part to G protein inhibition of Ca influx.
		inhibition was rapid (<1 s) and was attenuated by cleavage of synaptosome-associated protein of 25 kD (SNAP25).
		bound soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes, and binding was reduced to SNARE complexes containing cleaved SNAP25 or by Ca -dependent synaptotagmin binding.
	www.nature.com /neuro/journal/v8/n4/abs/nn1423.html;jsessionid=BB3FE2AFEA87124EE5A06FDB769729FD (272 words)

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