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BET1 Bet1p

BET1, Bet1p, rbet1
protein involved with vesicular membrane traffic, especially with the golgi; may be associated with the SNARE complex [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Bos1p, CAN, v-SNARE, STEP, Ykt6
Papers using BET1 antibodies
Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability
Lupashin Vladimir et al., In The Journal of Cell Biology, 2004
... 1:1,000); mouse anti-GM130 (WB 1:500; IF 1:250); anti–human GS28 (WB 1:500; IF 1:100; BD Biosciences); anti-Bet1 (WB 1:200; BD Biosciences); anti–protein disulfide isomerase (WB ...
Papers on BET1
Overexpression of native Saccharomyces cerevisiae ER-to-Golgi SNARE genes increased heterologous cellulase secretion.
Van Zyl et al., Stellenbosch, South Africa. In Appl Microbiol Biotechnol, Jan 2016
We have demonstrated an increase in secretory titers for the Talaromyces emersonii Cel7A (Te-Cel7A, a cellobiohydrolase) and the Saccharomycopsis fibuligera Cel3A (Sf-Cel3A, a β-glucosidase) expressed in Saccharomyces cerevisiae through single and co-overexpression of some of the endoplasmic reticulum (ER)-to-Golgi SNAREs (BOS1, BET1, SEC22 and SED5).
A randomised, double-blind trial comparing budesonide formulations and dosages for short-term treatment of eosinophilic oesophagitis.
Straumann et al., Hamburg, Germany. In Gut, Apr 2015
DESIGN: Adults with active EoE (n=76) randomly received 14 days' treatment with either BET 2×1 mg/day (BET1, n=19) or BET 2×2 mg/day (BET2, n=19), or BVS 2×5 mL (0.4 mg/mL)/day (BVS, n=19) or placebo (n=19) in a double-blind, double-dummy fashion, with a 2-week follow-up.
p115-SNARE interactions: a dynamic cycle of p115 binding monomeric SNARE motifs and releasing assembled bundles.
Hay et al., Missoula, United States. In Traffic, Feb 2015
Using a gel filtration binding assay, we have demonstrated that in solution p115 stably interacts with ER/Golgi SNAREs rbet1 and sec22b, but not membrin and syntaxin 5.
The postprandial chylomicron triacylglycerol response to dietary fat in healthy male adults is significantly explained by a combination of single nucleotide polymorphisms in genes involved in triacylglycerol metabolism.
Borel et al., Marseille, France. In J Clin Endocrinol Metab, 2014
RESULTS: Data obtained allowed us to generate a validated significant model (P = 1.3 × 10(-7)) that included 42 SNPs in 23 genes (ABCA1, APOA1, APOA5, APOB, BET1, CD36, COBLL1, ELOVL5, FRMD5, GPAM, INSIG2, IRS1, LDLR, LIPC, LPL, LYPLAL1, MC4R, NAT2, PARK2, SLC27A5, SLC27A6, TCF7L2, and ZNF664) and explained 88% of the variance.
The identification of the SNARE complex required for the fusion of VLDL-transport vesicle with hepatic cis-Golgi.
Siddiqi et al., Orlando, United States. In Biochem J, 2010
The components of the complex were identified as Sec22b, syntaxin 5, rBet1 and GOS28.
Choline metabolism in glycinebetaine accumulating and non-accumulating near-isogenic lines of Zea mays and Sorghum bicolor.
Rhodes et al., West Lafayette, United States. In Phytochemistry, 2010
The previously identified bet1 locus does not appear to be choline monooxygenase.
TGF-beta1 and C-erb-B2 neu oncoprotein in Egyptian HCV related chronic liver disease and hepatocellular carcinoma patients.
Shaker et al., Egypt. In Egypt J Immunol, 2007
Significant difference were obtained when comparing TGF-bet1 and C-erb-B2 mRNA in HCV and HCC P = 0.0076, and controls.
The identification of a novel endoplasmic reticulum to Golgi SNARE complex used by the prechylomicron transport vesicle.
Mansbach et al., Memphis, United States. In J Biol Chem, 2006
PCTV, docked with cis-Golgi, were solubilized in 2% Triton X-100, and proteins were immunoprecipitated using VAMP7 or rBet1 antibodies.
Vesicle-associated membrane protein 7 is expressed in intestinal ER.
Mansbach et al., Memphis, United States. In J Cell Sci, 2006
Immunoelectron microscopy showed that the ER proteins Sar1 and rBet1 were present on PCTVs and colocalized with VAMP7.
Cysteine-disulfide cross-linking to monitor SNARE complex assembly during endoplasmic reticulum-Golgi transport.
Barlowe et al., United States. In J Biol Chem, 2006
In Saccharomyces cerevisiae, anterograde ER-Golgi transport requires four SNARE proteins: Sec22p, Bos1p, Bet1p, and Sed5p.
Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles.
Schekman et al., Berkeley, United States. In Cell, 2003
We identified a site on Sec24p that recognizes the v-SNARE Bet1p and show that packaging of a number of cargo molecules is disrupted when mutations are introduced at this site.
The SNARE motif contributes to rbet1 intracellular targeting and dynamics independently of SNARE interactions.
Hay et al., Ann Arbor, United States. In J Biol Chem, 2003
SNARE motif contributes to rbet1 intracellular targeting and dynamics independently of SNARE interactions
GS15 forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is implicated in traffic in the early cisternae of the Golgi apparatus.
Hong et al., Singapore, Singapore. In Mol Biol Cell, 2002
Data suggest that GS15 exists in a distinct SNARE complex that contains syntaxin5, GS28, and Ykt6, and may be involved in both ER-to-Golgi and intra-Golgi transport.
Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles.
Klumperman et al., Utrecht, Netherlands. In Cell, 1999
We have determined the concentrations of the secretory proteins amylase and chymotrypsinogen and the membrane proteins KDELr and rBet1 in COPII- and COPI-coated pre-Golgi compartments of pancreatic cells by quantitative immunoelectron microscopy.
Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs.
Schekman et al., Berkeley, United States. In Science, 1998
Here, two ER to Golgi v-SNAREs, Bet1p and Bos1p, were shown to interact specifically with Sar1p, Sec23p, and Sec24p, components of the COPII coat, in a guanine nucleotide-dependent fashion.
Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells.
Scheller et al., Stanford, United States. In Cell, 1997
The proposed cis-Golgi vesicle receptor syntaxin 5 was found in a complex with Golgi-associated SNARE of 28 kDa (GOS-28), rbet1, rsly1, and two novel proteins characterized herein: rat sec22b and membrin, both cytoplasmically oriented integral membrane proteins.
Mammalian vesicle trafficking proteins of the endoplasmic reticulum and Golgi apparatus.
Scheller et al., Stanford, United States. In J Biol Chem, 1996
The distinct localizations of rsec22 and rbet1 may reflect their participation in opposite directions of membrane flow between the endoplasmic reticulum and Golgi apparatus.
Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence.
Ferro-Novick et al., New Haven, United States. In Cell, 1993
BOS1 encodes an integral endoplasmic reticulum (ER) membrane protein and genetically interacts with three other yeast genes (BET1, SEC22, and YPT1) whose products are required for membrane traffic between the ER and the Golgi apparatus.
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