Alternative titles; symbols
HGNC Approved Gene Symbol: GOSR1
Cytogenetic location: 17q11.2 Genomic coordinates (GRCh38) : 17:30,477,408-30,527,592 (from NCBI)
SNARE proteins play indispensable roles in membrane fusion events in various cell processes, including synaptic transmission and protein trafficking. SNAREs are functionally classified as either v-SNAREs, which are anchored into transport vesicles, or t-SNAREs, which are tethered to the target compartment. When a vesicle docks with its target compartment, membrane fusion is mediated by formation of a SNARE complex involving a single v-SNARE on the vesicle and 3 t-SNAREs on the target membrane. GOSR1 is a Golgi SNARE involved in a variety of transport steps, including anterograde transport between the endoplasmic reticulum (ER) and Golgi, intra-Golgi transport in both directions, and retrograde transport for the early/recycling endosome back to the trans-Golgi network. Moreover, GOSR1 has been reported to function as both a v-SNARE and a t-SNARE (summary by Rosenbaum et al., 2014).
Nagahama et al. (1996) cloned Gosr1, which they called Gos28, from a Chinese hamster ovary (CHO) cell line. The deduced 250-amino acid protein has a calculated molecular mass of 28.5 kD. It lacks an N-terminal signal sequence, but it has a possible N-terminal coiled-coil region and a possible C-terminal hydrophobic domain that may act as a membrane anchor. Immunofluorescence and immunoelectron microscopy of CHO cells localized epitope-tagged Gos28 to the Golgi apparatus, with enrichment of vesicular components at terminal rims of Golgi cisternae.
Subramaniam et al. (1996) isolated cDNAs encoding rat Gos28, which they called p28 or Gs28. The predicted protein contains a central coiled-coil domain and a C-terminal membrane anchor.
By searching EST databases using the rat GS28 protein sequence, Bui et al. (1999) identified human GS28 cDNAs. The deduced 250-amino acid human protein is 97% identical to rat GS28. Independently, Mao et al. (1998) identified a human GOS28 cDNA among a collection of cDNAs expressed in hematopoietic stem/progenitor cells.
Rosenbaum et al. (2014) described a 248-amino acid isoform of human GOS28 that has 3 putative helical domains near the N terminus, followed by a SNARE motif and a C-terminal transmembrane domain. Western blot analysis of human retinal tissue detected GOS28 at an apparent molecular mass of 28 kD.
Using an anti-Gos28 antibody, Nagahama et al. (1996) found that inactivation of Gos28 in CHO cells blocked binding of Gos28 to alpha-Snap (NAPA; 603215) in a dose-dependent manner, inhibited cis- to medial-Golgi transport, and caused accumulation of uncoated docked vesicles. Nagahama et al. (1996) concluded that complexes containing Gos28 are required for Golgi vesicle fusion after docking.
Subramaniam et al. (1996) identified rat Gs28 as a core component of the Golgi 20S SNARE complex that participates in the docking or fusion stage of ER-Golgi transport.
Lowe et al. (1997) reported that GS28 plays a role in transport from the ER to the cis- (inside face) and medial-Golgi, while the GS27 (604027) Golgi SNARE participates in protein movement from the medial-Golgi towards the trans-Golgi (plasma-membrane face) and the trans-Golgi network.
Rosenbaum et al. (2014) found that gos28 was required for vesicular transport of rhodopsin (RHO; 180380), or rh1, via the secretory pathway in Drosophila photoreceptor cells. Gos28 functioned as a t-SNARE during trafficking of rh1 through distal Golgi compartments. Null mutations in gos28 led to defective trafficking of rh1, accumulation of membranes in the secretory pathway, and retinal degeneration. Loss of gos28 did not alter assembly of functional SNARE complexes or inhibit membrane fusion. Deletion analysis revealed that the N terminus of gos28, including the SNARE motif, was sufficient to facilitate rh1 transport. Human GOS28, which shares 43% amino acid identity with Drosophila gos28, rescued rh1 trafficking and retinal degeneration in gos28-null retina.
By analysis of radiation hybrids and by fluorescence in situ hybridization, Bui et al. (1999) mapped the GS28 gene to chromosome 17q11.
Bui, T. D., Levy, E. R., Subramaniam, V. N., Lowe, S. L., Hong, W. cDNA characterization and chromosomal mapping of human Golgi SNARE GS27 and GS28 to chromosome 17. Genomics 57: 285-288, 1999. [PubMed: 10198168] [Full Text: https://doi.org/10.1006/geno.1998.5649]
Lowe, S. L., Peter, F., Subramaniam, V. N., Wong, S. H., Hong, W. A SNARE involved in protein transport through the Golgi apparatus. Nature 389: 881-884, 1997. [PubMed: 9349823] [Full Text: https://doi.org/10.1038/39923]
Mao, M., Fu, G., Wu, J.-S., Zhang, Q.-H., Zhou, J., Kan, L.-X., Huang, Q.-H., He, K.-L., Gu, B.-W., Han, Z.-G., Shen, Y., Gu, J., Yu, Y.-P., Xu, S.-H., Wang, Y.-X., Chen, S.-J., Chen, Z. Identification of genes expressed in human CD34+ hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning. Proc. Nat. Acad. Sci. 95: 8175-8180, 1998. [PubMed: 9653160] [Full Text: https://doi.org/10.1073/pnas.95.14.8175]
Nagahama, M., Orci, L., Ravazzola, M., Amherdt, M., Lacomis, L., Tempst, P., Rothman, J. E., Sollner, T. H. A v-SNARE implicated in intra-Golgi transport. J. Cell Biol. 133: 507-516, 1996. [PubMed: 8636227] [Full Text: https://doi.org/10.1083/jcb.133.3.507]
Rosenbaum, E. E., Vasiljevic, E., Cleland, S. C., Flores, C., Colley, N. J. The Gos28 SNARE protein mediates intra-Golgi transport of rhodopsin and is required for photoreceptor survival. J. Biol. Chem. 289: 32392-32409, 2014. [PubMed: 25261468] [Full Text: https://doi.org/10.1074/jbc.M114.585166]
Subramaniam, V. N., Peter, F., Philp, R., Wong, S. H., Hong, W. GS28, a 28-kilodalton Golgi SNARE that participates in ER-Golgi transport. Science 272: 1161-1163, 1996. [PubMed: 8638159] [Full Text: https://doi.org/10.1126/science.272.5265.1161]