Jump to content

STX6

From Wikipedia, the free encyclopedia

STX6
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSTX6, syntaxin 6
External IDsOMIM: 603944; MGI: 1926235; HomoloGene: 115622; GeneCards: STX6; OMA:STX6 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001286210
NM_005819

NM_021433

RefSeq (protein)

NP_001273139
NP_005810

NP_067408

Location (UCSC)Chr 1: 180.97 – 181.02 MbChr 1: 155.03 – 155.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Syntaxin-6 is a protein that in humans is encoded by the STX6 gene.[5][6]

Interactions

[edit]

STX6 has been shown to interact with SNAP23,[7] VAMP3[8] and VAMP4.[8]

N terminal protein domain

[edit]

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.[9]

Structure

[edit]

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.[10]

Function

[edit]

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.[10]

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000135823Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026470Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ "Entrez Gene: STX6 syntaxin 6".
  7. ^ 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.
  8. ^ a b 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.
  9. ^ 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.
  10. ^ a b 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

[edit]
[edit]