STX8

Syntaxin-8 is a protein that in humans is encoded by the STX8 gene.[5][6][7] Syntaxin 8 directly interacts with HECTd3 and has similar subcellular localization.[8] The protein has been shown to form the SNARE complex with syntaxin 7, vti1b and endobrevin. These function as the machinery for the homotypic fusion of late endosomes.[9]

STX8
Identifiers
Aliases	STX8, CARB, syntaxin 8
External IDs	OMIM: 604203 MGI: 1890156 HomoloGene: 37973 GeneCards: STX8
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p13.1 Start 9,250,471 bp[1] End 9,576,591 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 B3 Start 67,966,193 bp[2] End 68,207,148 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • SNAP receptor activity • GO:0001948 protein binding • chloride channel inhibitor activity • syntaxin binding • ubiquitin protein ligase binding • SNARE binding Cellular component • integral component of membrane • recycling endosome • vesicle • endosome • late endosome • membrane • late endosome membrane • integral component of plasma membrane • lysosomal membrane • trans-Golgi network • early endosome • endoplasmic reticulum • perinuclear region of cytoplasm • cytosol • SNARE complex • phagocytic vesicle • endomembrane system Biological process • endosome to lysosome transport • vesicle docking • early endosome to late endosome transport • intracellular protein transport • vesicle-mediated transport • regulation of protein localization to plasma membrane • vesicle fusion • cellular response to interferon-gamma Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9482	55943
Ensembl	ENSG00000170310	ENSMUSG00000020903
UniProt	Q9UNK0	O88983
RefSeq (mRNA)	NM_004853	NM_018768 NM_001356314 NM_001361350 NM_001361351 NM_001361352
RefSeq (protein)	NP_004844	NP_061238 NP_001343243 NP_001348279 NP_001348280 NP_001348281
Location (UCSC)	Chr 17: 9.25 – 9.58 Mb	Chr 11: 67.97 – 68.21 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Model organisms

Stx8 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Skin Histopathology	Normal
Brain histopathology	Normal
Eye Histopathology	Normal
Salmonella infection	Normal[10]
Citrobacter infection	Normal[11]
All tests and analysis from[12][13]

Model organisms have been used in the study of STX8 function. A conditional knockout mouse line, called Stx8^{tm2a(EUCOMM)Wtsi}[14][15] was generated as part of the International Knockout Mouse Consortium program—a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists—at the Wellcome Trust Sanger Institute.[16][17][18] Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[12][19] Twenty four tests were carried out on homozygous mutant adult mice, however no significant abnormalities were observed.[12]

Interactions

STX8 has been shown to interact with Vesicle-associated membrane protein 8,[20] VTI1B[21][22] and STX7.[20]

References

1. GRCh38: Ensembl release 89: ENSG00000170310 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020903 - 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. Steegmaier M, Yang B, Yoo JS, Huang B, Shen M, Yu S, Luo Y, Scheller RH (Dec 1998). "Three novel proteins of the syntaxin/SNAP-25 family". The Journal of Biological Chemistry. 273 (51): 34171–9. doi:10.1074/jbc.273.51.34171. PMID 9852078.
6. Thoreau V, Bergès T, Callebaut I, Guillier-Gencik Z, Gressin L, Bernheim A, Karst F, Mornon JP, Kitzis A, Chomel JC (Apr 1999). "Molecular cloning, expression analysis, and chromosomal localization of human syntaxin 8 (STX8)". Biochemical and Biophysical Research Communications. 257 (2): 577–83. doi:10.1006/bbrc.1999.0503. PMID 10198254.
7. "Entrez Gene: STX8 syntaxin 8".
8. Zhang L, Kang L, Bond W, Zhang N (Feb 2009). "Interaction between syntaxin 8 and HECTd3, a HECT domain ligase". Cellular and Molecular Neurobiology. 29 (1): 115–21. doi:10.1007/s10571-008-9303-0. PMID 18821010. S2CID 23216243.
9. Kasai K, Suga K, Izumi T, Akagawa K (October 2008). "Syntaxin 8 has two functionally distinct di-leucine-based motifs". Cellular & Molecular Biology Letters. 13 (1): 144–54. doi:10.2478/s11658-007-0043-9. PMC 6275627. PMID 17965969.
10. "Salmonella infection data for Stx8". Wellcome Trust Sanger Institute.
11. "Citrobacter infection data for Stx8". Wellcome Trust Sanger Institute.
12. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.
13. Mouse Resources Portal, Wellcome Trust Sanger Institute.
14. "International Knockout Mouse Consortium".
15. "Mouse Genome Informatics".
16. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
17. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
18. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015.
19. van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
20. Antonin W, Holroyd C, Fasshauer D, Pabst S, Von Mollard GF, Jahn R (Dec 2000). "A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function". The EMBO Journal. 19 (23): 6453–64. doi:10.1093/emboj/19.23.6453. PMC 305878. PMID 11101518.
21. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
22. Subramaniam VN, Loh E, Horstmann H, Habermann A, Xu Y, Coe J, Griffiths G, Hong W (Mar 2000). "Preferential association of syntaxin 8 with the early endosome". Journal of Cell Science. 113 ( Pt 6) (6): 997–1008. PMID 10683148.

Further reading

• Prekeris R, Yang B, Oorschot V, Klumperman J, Scheller RH (Nov 1999). "Differential roles of syntaxin 7 and syntaxin 8 in endosomal trafficking". Molecular Biology of the Cell. 10 (11): 3891–908. doi:10.1091/mbc.10.11.3891. PMC 25687. PMID 10564279.
• Subramaniam VN, Loh E, Horstmann H, Habermann A, Xu Y, Coe J, Griffiths G, Hong W (Mar 2000). "Preferential association of syntaxin 8 with the early endosome". Journal of Cell Science. 113 ( Pt 6) (6): 997–1008. PMID 10683148.
• McShea A, Samuel T, Eppel JT, Galloway DA, Funk JO (Jul 2000). "Identification of CIP-1-associated regulator of cyclin B (CARB), a novel p21-binding protein acting in the G2 phase of the cell cycle". The Journal of Biological Chemistry. 275 (30): 23181–6. doi:10.1074/jbc.M001772200. PMID 10781590.
• 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.
• Antonin W, Holroyd C, Fasshauer D, Pabst S, Von Mollard GF, Jahn R (Dec 2000). "A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function". The EMBO Journal. 19 (23): 6453–64. doi:10.1093/emboj/19.23.6453. PMC 305878. PMID 11101518.
• Wade N, Bryant NJ, Connolly LM, Simpson RJ, Luzio JP, Piper RC, James DE (Jun 2001). "Syntaxin 7 complexes with mouse Vps10p tail interactor 1b, syntaxin 6, vesicle-associated membrane protein (VAMP)8, and VAMP7 in b16 melanoma cells". The Journal of Biological Chemistry. 276 (23): 19820–7. doi:10.1074/jbc.M010838200. PMID 11278762.
• Antonin W, Fasshauer D, Becker S, Jahn R, Schneider TR (Feb 2002). "Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs". Nature Structural Biology. 9 (2): 107–11. doi:10.1038/nsb746. hdl:11858/00-001M-0000-0012-F459-F. PMID 11786915. S2CID 17724790.
• Bogdanovic A, Bennett N, Kieffer S, Louwagie M, Morio T, Garin J, Satre M, Bruckert F (Nov 2002). "Syntaxin 7, syntaxin 8, Vti1 and VAMP7 (vesicle-associated membrane protein 7) form an active SNARE complex for early macropinocytic compartment fusion in Dictyostelium discoideum". The Biochemical Journal. 368 (Pt 1): 29–39. doi:10.1042/BJ20020845. PMC 1222979. PMID 12175335.
• Xu Y, Martin S, James DE, Hong W (Oct 2002). "GS15 forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is implicated in traffic in the early cisternae of the Golgi apparatus". Molecular Biology of the Cell. 13 (10): 3493–507. doi:10.1091/mbc.E02-01-0004. PMC 129961. PMID 12388752.
• Kim BY, Ueda M, Kominami E, Akagawa K, Kohsaka S, Akazawa C (Nov 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.
• Zhu X, McShea A, Harris PL, Raina AK, Castellani RJ, Funk JO, Shah S, Atwood C, Bowen R, Bowser R, Morelli L, Perry G, Smith MA (Mar 2004). "Elevated expression of a regulator of the G2/M phase of the cell cycle, neuronal CIP-1-associated regulator of cyclin B, in Alzheimer's disease". Journal of Neuroscience Research. 75 (5): 698–703. doi:10.1002/jnr.20028. PMID 14991845.
• Bilan F, Thoreau V, Nacfer M, Dérand R, Norez C, Cantereau A, Garcia M, Becq F, Kitzis A (Apr 2004). "Syntaxin 8 impairs trafficking of cystic fibrosis transmembrane conductance regulator (CFTR) and inhibits its channel activity". Journal of Cell Science. 117 (Pt 10): 1923–35. doi:10.1242/jcs.01070. PMID 15039462.
• Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (Mar 2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.