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Syntaxin 5

syntaxin 5
This gene encodes a member of the syntaxin or t-SNARE (target-SNAP receptor) family. These proteins are found on cell membranes and serve as the targets for v-SNAREs (vesicle-SNAP receptors), permitting specific synaptic vesicle docking and fusion. The encoded protein regulates endoplasmic reticulum to Golgi transport and plays a critical role in autophagy. Autoantibodies targeting the encoded protein may be a diagnostic marker for endometriosis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Sep 2011] (from NCBI)
Top mentioned proteins: CAN, CIs, BET1, Sec22b, STEP
Papers on syntaxin 5
SNARE-mediated cholesterol movement to mitochondria supports steroidogenesis in rodent cells.
Kraemer et al., Palo Alto, United States. In Mol Endocrinol, Feb 2016
Our results from reconstitution experiments along with knockdown studies in rat primary granulosa cells and in a Leydig cell line show that NSFα, SNAP25, syntaxin-5 and syntaxin-17 facilitate the transport of cholesterol to mitochondria.
Data supporting ER stress response in NG108-15 cells involves upregulation of syntaxin 5 expression and reduced amyloid β peptide secretion.
Akagawa et al., Kami-renjaku, Japan. In Data Brief, Dec 2015
This data contains insights into the upregulation of the ER-Golgi-soluble N-ethylmaleimide-sensitive factor-attachment protein receptors (ER-Golgi SNAREs) syntaxin 5 (Syx5) by ER stress and the downregulation of Syx5 by apoptosis induction.
Data for the effects of ER and Golgi stresses on the ER-Golgi SNARE Syntaxin5 expression and on the βAPP processing in cultured hippocampal neurons.
Akagawa et al., Kami-renjaku, Japan. In Data Brief, Dec 2015
This paper reports the data for the effects of organelle stresses on the ER-Golgi-soluble N-ethylmaleimide-sensitive factor-attachment protein receptors (ER-Golgi SNAREs) syntaxin 5 (Syx5) in neuronal cells.
A Conserved Structural Motif Mediates Retrograde Trafficking of Shiga Toxin Types 1 and 2.
Mukhopadhyay et al., Austin, United States. In Traffic, Dec 2015
Despite this difference, similar to STx1B, endosome-to-Golgi transport of STx2B does not involve transit through degradative late endosomes and is dependent on dynamin II, epsinR, retromer and syntaxin5.
The Q-soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor (Q-SNARE) SNAP-47 Regulates Trafficking of Selected Vesicle-associated Membrane Proteins (VAMPs).
Proux-Gillardeaux et al., Paris, France. In J Biol Chem, Dec 2015
SNAP-47 also interacted with ER and Golgi syntaxin 5 and with syntaxin 1 in the absence of Munc18a, when syntaxin 1 is retained in the ER.
ER stress response in NG108-15 cells involves upregulation of syntaxin 5 expression and reduced amyloid β peptide secretion.
Akagawa et al., Kami-renjaku, Japan. In Exp Cell Res, Apr 2015
We previously showed that manipulation of the ER-Golgi-soluble N-ethylmaleimide-sensitive factor-attachment protein receptors (ER-Golgi SNARE) syntaxin 5 (Syx5) causes changes in Golgi morphology and the processing of AD-related proteins.
The formation of lipid droplets: possible role in the development of insulin resistance/type 2 diabetes.
Boström et al., Göteborg, Sweden. In Prostaglandins Leukot Essent Fatty Acids, 2011
The fusion is catalyzed by the SNARE proteins SNAP23, syntaxin-5 and VAMP4.
Identification of anti-syntaxin 5 autoantibody as a novel serum marker of endometriosis.
Ito et al., Japan. In J Reprod Immunol, 2011
serum anti-STX5 autoantibody, which was discovered by a proteomic approach, is a potential new serum marker for the diagnosis of endometriosis.
Retracted: 147 reduced syntaxin-5 in skeletal muscle of patients with type 2 diabetes. A link between lipid storage and insulin resistance.
Olofsson et al., In Atheroscler Suppl, 2011
This article has been retracted: please see Elsevier Policy on Article Withdrawal (
Autophagic substrate clearance requires activity of the syntaxin-5 SNARE complex.
Rubinsztein et al., Cambridge, United Kingdom. In J Cell Sci, 2011
Depletion of syntaxin-5 complex components results in the accumulation of autophagosomes as a result of lysosomal dysfunction, leading to decreased degradation of autophagic substrates.
The assembly of lipid droplets and its relation to cellular insulin sensitivity.
Olofsson et al., Göteborg, Sweden. In Biochem Soc Trans, 2009
Lipid droplets grow in size by fusion, which is dependent on dynein and the transfer on microtubules, and is catalysed by the SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) proteins SNAP-23 (23 kDa synaptosome-associated protein), syntaxin-5 and VAMP-4 (vesicle-associated protein 4).
Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing.
Lev et al., Israel. In Embo J, 2009
Study shows that the SM protein, Sly1, interacts directly with the conserved oligomeric Golgi (COG) tethering complex; Sly1-COG interaction is mediated by the Cog4 subunit, which also interacts with Syntaxin 5 through a different binding site.
Coordination of golgin tethering and SNARE assembly: GM130 binds syntaxin 5 in a p115-regulated manner.
Lowe et al., Manchester, United Kingdom. In J Biol Chem, 2008
depletion of GM130 by RNA interference slows the rate of ER to Golgi trafficking in vivo; interactions of GM130 with syntaxin 5 and Rab1 are regulated by mitotic phosphorylation
SNARE proteins mediate fusion between cytosolic lipid droplets and are implicated in insulin sensitivity.
Olofsson et al., Göteborg, Sweden. In Nat Cell Biol, 2007
Here, we show that lipid droplets are associated with proteins involved in fusion processes in the cell: NSF (N-ethylmaleimide-sensitive-factor), alpha-SNAP (soluble NSF attachment protein) and the SNAREs (SNAP receptors), SNAP23 (synaptosomal-associated protein of 23 kDa), syntaxin-5 and VAMP4 (vesicle-associated membrane protein 4).
Syntaxin 16 and syntaxin 5 are required for efficient retrograde transport of several exogenous and endogenous cargo proteins.
Johannes et al., Paris, France. In J Cell Sci, 2007
hypothesize that syntaxin 5 also has trafficking-independent functions
p97/p47-Mediated biogenesis of Golgi and ER.
Kondo et al., Machida, Japan. In J Biochem, 2005
In the p97-mediated membrane fusion, p47 was identified as an essential cofactor, through which p97 binds to a SNARE, syntaxin5.
SNAREs and membrane fusion in the Golgi apparatus.
Pelham et al., Cambridge, United Kingdom. In Biochim Biophys Acta, 1998
The best characterised SNAREs in the Golgi are Sed5p in yeast and its mammalian homologue syntaxin 5, both of which are predominantly localised to the cis Golgi.
Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro.
Warren et al., London, United Kingdom. In Cell, 1998
Anti-syntaxin 5 antibodies and a soluble, recombinant syntaxin 5 inhibited both pathways, suggesting that this t-SNARE is a common component.
Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates.
Balch et al., Los Angeles, United States. In Science, 1998
Here, syntaxin 5 (Syn5) was shown to be an integral component of endoplasmic reticulum-derived transport vesicles.
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.
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