Giantin
| GOLGB1 | |||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | GOLGB1, GCP, GCP372, GOLIM1, golgin B1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 602500; MGI: 1099447; HomoloGene: 68401; GeneCards: GOLGB1; OMA:GOLGB1 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
Giantin or Golgin subfamily B member 1 is a protein that in humans is encoded by the GOLGB1 gene.[5][6][7] Giantin is a component of the Golgi matrix that localizes to the cis-medial rims of the Golgi apparatus. It functions in membrane trafficking within the secretory pathway, contributing to the correct localization of proteins at the plasma membrane and in the extracellular space, thereby supporting receptor function and extracellular matrix organization.
Structure
[edit]Giantin is a disulfide-linked homodimer containing approximately 37 coiled-coil domains. The protein is localized to the cis-medial rims of the Golgi and forms part of the Golgi matrix.[8]
Function
[edit]Giantin functions as a Golgi matrix protein involved in membrane trafficking through the secretory pathway. It contributes to the proper targeting of proteins to the plasma membrane and extracellular space, processes that are essential for normal receptor function and maintenance of the extracellular matrix.
Giantin interacts with several proteins involved in Golgi organization and vesicle trafficking. It has been shown to interact with ACBD3, PLK3,[8] and the vesicle-tethering small GTPases Rab1 and Rab6.[9] Giantin also binds P115 through its N-terminal coiled-coil domains, facilitating interaction with the Golgi matrix protein GM130, a complex thought to be important for Golgi secretory function.[10]
Loss-of-function studies have also implicated giantin in the function of primary cilia,[11][12] as well as in the regulation of glycosyltransferase expression and calcineurin signaling in cultured cells.[13][14]
Clinical significance
[edit]Knockout studies of GOLGB1 in mice,[15] rats,[16] and zebrafish[11] have demonstrated species-specific phenotypes ranging from mild to severe craniofacial abnormalities in rodents to relatively minor developmental defects in zebrafish. Adult zebrafish lacking giantin develop a tumoral calcinosis-like phenotype, which resembles the human disorder associated with defects in glycosyltransferase function, including mutations affecting GALNT3.[13]
References
[edit]- 1 2 3 GRCh38: Ensembl release 89: ENSG00000173230 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000034243 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Linstedt AD, Hauri HP (November 1993). "Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa". Molecular Biology of the Cell. 4 (7): 679–693. doi:10.1091/mbc.4.7.679. PMC 300978. PMID 7691276.
- ↑ Oka T, Ungar D, Hughson FM, Krieger M (April 2004). "The COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteins". Molecular Biology of the Cell. 15 (5): 2423–2435. doi:10.1091/mbc.E03-09-0699. PMC 404034. PMID 15004235.
- ↑ "Entrez Gene: GOLGB1 golgi autoantigen, golgin subfamily b, macrogolgin (with transmembrane signal), 1". Archived from the original on 2010-12-05. Retrieved 2017-08-31.
- 1 2 Sohda M, Misumi Y, Yamamoto A, Yano A, Nakamura N, Ikehara Y (November 2001). "Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin". The Journal of Biological Chemistry. 276 (48): 45298–45306. doi:10.1074/jbc.M108961200. PMID 11590181.
- ↑ Rosing M, Ossendorf E, Rak A, Barnekow A (July 2007). "Giantin interacts with both the small GTPase Rab6 and Rab1". Experimental Cell Research. 313 (11): 2318–2325. doi:10.1016/j.yexcr.2007.03.031. PMID 17475246. Archived from the original on 2020-02-12.
- ↑ Brandon E, Gao Y, Garcia-Mata R, Alvarez C, Sztul E (August 2003). "Membrane targeting of p115 phosphorylation mutants and their effects on Golgi integrity and secretory traffic". European Journal of Cell Biology. 82 (8): 411–420. doi:10.1078/0171-9335-00327. PMID 14533739. Archived from the original on 2018-06-03.
- 1 2 Bergen DJ, Stevenson NL, Skinner RE, Stephens DJ, Hammond CL (August 2017). "The Golgi matrix protein giantin is required for normal cilia function in zebrafish". Biology Open. 6 (8): 1180–1189. doi:10.1242/bio.025502. PMC 5576078. PMID 28546340.
- ↑ Asante D, MacCarthy-Morrogh L, Townley AK, Weiss MA, Katayama K, Palmer KJ, et al. (November 2013). "A role for the Golgi matrix protein giantin in ciliogenesis through control of the localization of dynein-2". Journal of Cell Science. 126 (Pt 22): 5189–5197. doi:10.1242/jcs.131664. PMC 3828591. PMID 24046448.
- 1 2 Stevenson NL, Bergen DJ, Skinner RE, Kague E, Martin-Silverstone E, Robson Brown KA, et al. (December 2017). "Giantin-knockout models reveal a feedback loop between Golgi function and glycosyltransferase expression". Journal of Cell Science. 130 (24): 4132–4143. doi:10.1242/jcs.212308. PMC 5769581. PMID 29093022.
- ↑ Stevenson NL, Bergen DJ, Xu A, Wyatt E, Henry F, McCaughey J, et al. (May 2018). "Regulator of calcineurin-2 is a centriolar protein with a role in cilia length control". Journal of Cell Science. 131 (9) jcs212258. doi:10.1242/jcs.212258. PMC 5992583. PMID 29643119.
- ↑ Lan Y, Zhang N, Liu H, Xu J, Jiang R (July 2016). "Golgb1 regulates protein glycosylation and is crucial for mammalian palate development". Development. 143 (13). Cambridge, England: 2344–2355. doi:10.1242/dev.134577. PMC 4958322. PMID 27226319.
- ↑ Katayama K, Sasaki T, Goto S, Ogasawara K, Maru H, Suzuki K, et al. (November 2011). "Insertional mutation in the Golgb1 gene is associated with osteochondrodysplasia and systemic edema in the OCD rat". Bone. 49 (5): 1027–1036. doi:10.1016/j.bone.2011.08.001. PMID 21851869. Archived from the original on 2022-01-27.
Further reading
[edit]- Sohda M, Misumi Y, Fujiwara T, Nishioka M, Ikehara Y (December 1994). "Molecular cloning and sequence analysis of a human 372-kDA protein localized in the Golgi complex". Biochemical and Biophysical Research Communications. 205 (2): 1399–1408. doi:10.1006/bbrc.1994.2821. PMID 7802676.
- Seelig HP, Schranz P, Schröter H, Wiemann C, Renz M (February 1994). "Macrogolgin--a new 376 kD Golgi complex outer membrane protein as target of antibodies in patients with rheumatic diseases and HIV infections". Journal of Autoimmunity. 7 (1): 67–91. doi:10.1006/jaut.1994.1006. PMID 8198703.
- Sönnichsen B, Lowe M, Levine T, Jämsä E, Dirac-Svejstrup B, Warren G (March 1998). "A role for giantin in docking COPI vesicles to Golgi membranes". The Journal of Cell Biology. 140 (5): 1013–1021. doi:10.1083/jcb.140.5.1013. PMC 2132694. PMID 9490716.
- Linstedt AD, Jesch SA, Mehta A, Lee TH, Garcia-Mata R, Nelson DS, et al. (April 2000). "Binding relationships of membrane tethering components. The giantin N terminus and the GM130 N terminus compete for binding to the p115 C terminus". The Journal of Biological Chemistry. 275 (14): 10196–10201. doi:10.1074/jbc.275.14.10196. PMID 10744704.
- Dirac-Svejstrup AB, Shorter J, Waters MG, Warren G (2000). "Phosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragments". The Journal of Cell Biology. 150 (3): 475–488. doi:10.1083/jcb.150.3.475. PMC 2175190. PMID 10931861.
- Alvarez C, Garcia-Mata R, Hauri HP, Sztul E (2001). "The p115-interactive proteins GM130 and giantin participate in endoplasmic reticulum-Golgi traffic". The Journal of Biological Chemistry. 276 (4): 2693–2700. doi:10.1074/jbc.M007957200. PMID 11035033.
- Shorter J, Beard MB, Seemann J, Dirac-Svejstrup AB, Warren G (April 2002). "Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115". The Journal of Cell Biology. 157 (1): 45–62. doi:10.1083/jcb.200112127. PMC 2173270. PMID 11927603.
- Gillingham AK, Pfeifer AC, Munro S (2003). "CASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantin". Molecular Biology of the Cell. 13 (11): 3761–3774. doi:10.1091/mbc.E02-06-0349. PMC 133590. PMID 12429822.
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, et al. (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Anderson NL, Polanski M, Pieper R, Gatlin T, Tirumalai RS, Conrads TP, et al. (April 2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources". Molecular & Cellular Proteomics. 3 (4): 311–326. doi:10.1074/mcp.M300127-MCP200. PMID 14718574.
- Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, et al. (July 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–1332. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
- Breuza L, Halbeisen R, Jenö P, Otte S, Barlowe C, Hong W, et al. (November 2004). "Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46". The Journal of Biological Chemistry. 279 (45): 47242–47253. doi:10.1074/jbc.M406644200. PMID 15308636.
- Malsam J, Satoh A, Pelletier L, Warren G (2005). "Golgin tethers define subpopulations of COPI vesicles". Science. 307 (5712). New York, N.Y.: 1095–1098. Bibcode:2005Sci...307.1095M. doi:10.1126/science.1108061. PMID 15718469. S2CID 12601850.
- Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, et al. (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–968. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
