STX6

Protein-coding gene in the species Homo sapiens
STX6
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2NPS, 4J2C

Identifiers
AliasesSTX6, syntaxin 6
External IDsOMIM: 603944; MGI: 1926235; HomoloGene: 115622; GeneCards: STX6; OMA:STX6 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for STX6
Genomic location for STX6
Band1q25.3Start180,972,712 bp[1]
End181,023,121 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for STX6
Genomic location for STX6
Band1|1 G3Start155,034,461 bp[2]
End155,084,002 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • endothelial cell

  • gingival epithelium

  • ganglionic eminence

  • Brodmann area 23

  • skin of thigh

  • skin of hip

  • monocyte

  • primary visual cortex

  • cartilage tissue
Top expressed in
  • external carotid artery

  • internal carotid artery

  • Rostral migratory stream

  • conjunctival fornix

  • epithelium of lens

  • medullary collecting duct

  • endocardial cushion

  • hair follicle

  • left lung lobe

  • Gonadal ridge
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • protein binding
  • syntaxin binding
  • SNAP receptor activity
  • SNARE binding
Cellular component
  • membrane
  • plasma membrane
  • SNARE complex
  • early endosome
  • phagocytic vesicle
  • perinuclear region of cytoplasm
  • clathrin-coated vesicle
  • trans-Golgi network
  • integral component of membrane
  • Golgi membrane
  • trans-Golgi network membrane
  • Golgi apparatus
  • nucleoplasm
  • cytosol
  • synaptic vesicle
  • integral component of synaptic vesicle membrane
  • endomembrane system
Biological process
  • endosome organization
  • regulation of protein localization
  • vesicle docking
  • retrograde transport, endosome to Golgi
  • Golgi vesicle transport
  • protein transport
  • vesicle fusion
  • Golgi ribbon formation
  • vesicle-mediated transport
  • intracellular protein transport
  • endocytic recycling
  • synaptic vesicle to endosome fusion
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10228

58244

Ensembl

ENSG00000135823

ENSMUSG00000026470

UniProt

O43752

Q9JKK1

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

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

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.[9]

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.[10]

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.[10]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000135823 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026470 – Ensembl, 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

  • Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Bock JB, Lin RC, Scheller RH (July 1996). "A new syntaxin family member implicated in targeting of intracellular transport vesicles". The Journal of Biological Chemistry. 271 (30): 17961–5. doi:10.1074/jbc.271.30.17961. PMID 8663448.
  • Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, et al. (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Simonsen A, Lippé R, Christoforidis S, Gaullier JM, Brech A, Callaghan J, et al. (July 1998). "EEA1 links PI(3)K function to Rab5 regulation of endosome fusion". Nature. 394 (6692): 494–8. Bibcode:1998Natur.394..494S. doi:10.1038/28879. PMID 9697774. S2CID 4305220.
  • Wong SH, Xu Y, Zhang T, Griffiths G, Lowe SL, Subramaniam VN, et al. (January 1999). "GS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6". Molecular Biology of the Cell. 10 (1): 119–34. doi:10.1091/mbc.10.1.119. PMC 25158. PMID 9880331.
  • Steegmaier M, Klumperman J, Foletti DL, Yoo JS, Scheller RH (June 1999). "Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking". Molecular Biology of the Cell. 10 (6): 1957–72. doi:10.1091/mbc.10.6.1957. PMC 25394. PMID 10359608.
  • Simonsen A, Gaullier JM, D'Arrigo A, Stenmark H (October 1999). "The Rab5 effector EEA1 interacts directly with syntaxin-6". The Journal of Biological Chemistry. 274 (41): 28857–60. doi:10.1074/jbc.274.41.28857. PMID 10506127.
  • Scales SJ, Chen YA, Yoo BY, Patel SM, Doung YC, Scheller RH (May 2000). "SNAREs contribute to the specificity of membrane fusion". Neuron. 26 (2): 457–64. doi:10.1016/S0896-6273(00)81177-0. PMID 10839363.
  • 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.
  • Wade N, Bryant NJ, Connolly LM, Simpson RJ, Luzio JP, Piper RC, James DE (June 2001). "Syntaxin 7 complexes with mouse Vps10p tail interactor 1b, syntaxin 6, vesicle-associated membrane protein (VAMP)8, and VAMP7 in b16 melanoma cells" (PDF). The Journal of Biological Chemistry. 276 (23): 19820–7. doi:10.1074/jbc.M010838200. PMID 11278762. S2CID 38183181.
  • Charest A, Lane K, McMahon K, Housman DE (August 2001). "Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6". The Journal of Biological Chemistry. 276 (31): 29456–65. doi:10.1074/jbc.M104137200. PMID 11384996.
  • Rotem-Yehudar R, Galperin E, Horowitz M (August 2001). "Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29". The Journal of Biological Chemistry. 276 (35): 33054–60. doi:10.1074/jbc.M009913200. PMID 11423532.
  • Cheng J, Moyer BD, Milewski M, Loffing J, Ikeda M, Mickle JE, et al. (February 2002). "A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression". The Journal of Biological Chemistry. 277 (5): 3520–9. doi:10.1074/jbc.M110177200. PMID 11707463.
  • 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.
  • Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J, Proux-Gillardeaux V, et al. (July 2003). "A dual mechanism controlling the localization and function of exocytic v-SNAREs". Proceedings of the National Academy of Sciences of the United States of America. 100 (15): 9011–6. Bibcode:2003PNAS..100.9011M. doi:10.1073/pnas.1431910100. PMC 166429. PMID 12853575.
  • Kim BY, Ueda M, Kominami E, Akagawa K, Kohsaka S, Akazawa C (November 2003). "Identification of mouse Vps16 and biochemical characterization of mammalian class C Vps complex". Biochemical and Biophysical Research Communications. 311 (3): 577–82. doi:10.1016/j.bbrc.2003.10.030. PMID 14623309.
  • Huynh H, Bottini N, Williams S, Cherepanov V, Musumeci L, Saito K, et al. (September 2004). "Control of vesicle fusion by a tyrosine phosphatase". Nature Cell Biology. 6 (9): 831–9. doi:10.1038/ncb1164. PMID 15322554. S2CID 25311826.

External links

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Synaptic vesicle
SNARE
Q-SNARE
R-SNARE
Synaptotagmin
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COPICOPIIRME/Clathrin
CaveolaeOther/ungrouped
Vesicle formation
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Adaptor protein complex 2:
Adaptor protein complex 3:
Adaptor protein complex 4:
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Small GTPase
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See also vesicular transport protein disorders