STX6

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An Error has occurred retrieving Wikidata item for infobox Syntaxin-6 is a protein that in humans is encoded by the STX6 gene.[1][2]

Interactions

STX6 has been shown to interact with SNAP23,[3] VAMP3[4] and VAMP4.[4]

N terminal protein domain

The protein domain Syntaxin 6 N terminal protein domain is a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) found in endosomal transport vesicles. It is part of the family, of target SNAREs (t-SNAREs). It is a vital aid to exporting and importing cell cargo through a process called cell trafficking. Its SNARE motif shows significant homology to both syntaxin 1a and S25C, indicating similarity through evolutionary conservation. The structure of the syntaxin 6 N-terminal domain shows strong structural similarity with the N-terminal domains of syntaxin 1a, Sso1p, and Vam3p; despite a very low level of sequence similarity. SNARE functions essentially as a tether to hold the vesicle. The cytoplasmic regions of SNARE found on transport vesicles and target membranes interact, then a four-helix coiled coil forms. This links the cell membrane and vesicles together in such a way that it overcomes the energetic barrier to fusing two lipid bilayers. This is the way cell cargo is exchanged. This particular entry focuses on the N-terminal domain of Syntaxin 6.[5]

Structure

Members of this entry, which are found in the amino terminus of various SNARE proteins, adopt a structure consisting of an antiparallel three-helix bundle. Their exact function has not been determined, though it is known that they regulate the SNARE motif, as well as mediate various protein-protein interactions involved in membrane-transport.[6]

Function

SNAREs play a vital role in the trafficking of cell cargo. The vesicles fuse to the cell membrane with the help of SNARE proteins. The SNARE motifs form a four-helix bundle that contributes to the fusion of two membranes. More specifically, the N-terminal domain binds to the SNARE motif, and this intramolecular interaction decreases the rate of association with the partner SNARE. However the N terminal domain's function still remains to fully elucidated.[6]

References

  1. Martín-Martín B, Nabokina SM, Lazo PA, Mollinedo F (March 1999). "Co-expression of several human syntaxin genes in neutrophils and differentiating HL-60 cells: variant isoforms and detection of syntaxin 1" (PDF). Journal of Leukocyte Biology. 65 (3): 397–406. doi:10.1002/jlb.65.3.397. hdl:10261/59829. PMID 10080545. S2CID 18988377.
  2. "Entrez Gene: STX6 syntaxin 6".
  3. Martín-Martín B, Nabokina SM, Blasi J, Lazo PA, Mollinedo F (October 2000). "Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis". Blood. 96 (7): 2574–83. doi:10.1182/blood.V96.7.2574. PMID 11001914.
  4. 4.0 4.1 Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, et al. (February 2002). "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform". The Journal of Cell Biology. 156 (4): 653–64. doi:10.1083/jcb.200110081. PMC 2174079. PMID 11839770.
  5. Jung JJ, Inamdar SM, Tiwari A, Choudhury A (August 2012). "Regulation of intracellular membrane trafficking and cell dynamics by syntaxin-6". Bioscience Reports. 32 (4): 383–91. doi:10.1042/BSR20120006. PMC 3392101. PMID 22489884.
  6. 6.0 6.1 Misura KM, Bock JB, Gonzalez LC, Scheller RH, Weis WI (July 2002). "Three-dimensional structure of the amino-terminal domain of syntaxin 6, a SNAP-25 C homolog". Proceedings of the National Academy of Sciences of the United States of America. 99 (14): 9184–9. doi:10.1073/pnas.132274599. PMC 123115. PMID 12082176.

Further reading

External links