Disease relevance of STX5

• Strikingly, a major decrease in Syx5 expression barely affected the anterograde transport of vesicular stomatitis virus G (VSVG) protein to the plasma membrane [1].

Psychiatry related information on STX5

• The PS1 variant linked to familial Alzheimer's disease (PS1DeltaE9), lacking the region that contains the endoproteolytic cleavage site in the cytoplasmic loop, showed markedly decreased binding to Syx5 [2].

High impact information on STX5

• Temperature shifts reveal that membrin, rsec22b, rbet1, and syntaxin 5 are present together on membranes that rapidly recycle between peripheral and Golgi-centric locations [3].
• In transfected cells, the N-terminal domain of Sly1 specifically disrupts the structure of the Golgi complex, supporting the notion that the interaction of Sly1 with syntaxin 5 is essential for fusion [4].
• We also report that GOS 28 and its partnering t-SNARE heavy chain, syntaxin 5, reside together in every cisterna of the stack [5].
• Here we demonstrate that antibodies against the endoplasmic reticulum/Golgi SNARE Syntaxin 5 inhibit COPII vesicle homotypic tethering as well as fusion, implying an unanticipated role for SNAREs upstream of fusion [6].
• The kinetics of inhibition exhibited by syntaxin 16 and syntaxin 5 antibodies is similar [7].

Chemical compound and disease context of STX5

• Under these conditions, vesicular stomatitis virus glycoprotein accumulated in pre-Golgi intermediates, which were strongly enriched in syntaxin 5 [8].

Biological context of STX5

• Our results indicate a central role for complexes among rbet1, rsec22b, membrin, and syntaxin 5 (34 and 41 kD) at two membrane fusion interfaces: the fusion of ER-derived vesicles with VTCs, and the assembly of VTCs to form cis-Golgi elements [3].
• Purified recombinant syntaxin 5, membrin, and rbet1, three Q-SNAREs, assemble cooperatively to create a high affinity binding site for sec22b, an R-SNARE [9].
• Caspase-mediated cleavage of syntaxin 5 and giantin accompanies inhibition of secretory traffic during apoptosis [10].
• We examined the effects of Syx5 down-regulation on the morphology of the Golgi apparatus and the transport of vesicles in mammalian cells [1].
• The deduced 301 amino-acid sequence of human syntaxin 5 shares 96% identity with rat syntaxin 5 [11].

Anatomical context of STX5

• Using co-immunoprecipitation, we found that PS bound to Syx5 (syntaxin 5), which is a target-soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor involved in endoplasmic reticulum (ER)-Golgi vesicular transport in vivo [2].
• Furthermore, Syx5 overexpression resulted in the accumulation of PS holoproteins and the beta-amyloid precursor protein, and reduced the secretion of the Abeta (amyloid beta) peptide in COS-7 cells [2].
• Syntaxin 5 is itself likely to cycle through the ER, and thus may be involved in homotypic fusion of ER derived transport vesicles [12].
• Sed5p and syntaxin 5 may mediate three distinct pathways for membrane flow into the cis Golgi, one from the ER, one from later Golgi cisternae, and possibly a third from endosomes [12].

Associations of STX5 with chemical compounds

• Immunofluorescence and sucrose-density-gradient fractionation analyses showed that the full-length PS holoproteins co-localized with Syx5 to the ER and cis-Golgi compartments [2].

Physical interactions of STX5

• Syntaxin 5 interacts with presenilin holoproteins, but not with their N- or C-terminal fragments, and affects beta-amyloid peptide production [2].

Other interactions of STX5

• The PS holoproteins co-immunoprecipitated with the mutant Syx5, which localized to the ER and Golgi compartments, despite the substitution of the transmembrane region with that of syntaxin 1A [2].
• Cloning and identification of human syntaxin 5 as a synaptobrevin/VAMP binding protein [11].
• Cleavage of giantin and syntaxin 5 is accompanied by a cessation of vesicular transport between the ER and the Golgi complex, which first manifests itself as a block in ER exit [10].
• Overexpression of the myc-tagged protein resulted in an anomalous staining pattern of SNARE molecules participating in ER-Golgi transport such as syntaxin 5 and mammalian bet1, but not the endosomal SNARE syntaxin 7 [13].

Analytical, diagnostic and therapeutic context of STX5

• We have cloned a 1557-bp cDNA that encodes the human syntaxin 5 isoform, using a combination of PCR and colony-screening methods [11].

References