STX6

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Protein-coding gene in the species Homo sapiens

title: "STX6" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in the species Homo sapiens" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/STX6" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Syntaxin-6 is a protein that in humans is encoded by the STX6 gene.

Interactions

STX6 has been shown to interact with SNAP23, VAMP3 and VAMP4.

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.

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.

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.

References

References

  1. (March 1999). "Co-expression of several human syntaxin genes in neutrophils and differentiating HL-60 cells: variant isoforms and detection of syntaxin 1". Journal of Leukocyte Biology.
  2. "Entrez Gene: STX6 syntaxin 6".
  3. (October 2000). "Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis". Blood.
  4. (February 2002). "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform". The Journal of Cell Biology.
  5. (August 2012). "Regulation of intracellular membrane trafficking and cell dynamics by syntaxin-6". Bioscience Reports.
  6. (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.

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