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Giantin

From Wikipedia, the free encyclopedia

GOLGB1
Identifiers
AliasesGOLGB1, GCP, GCP372, GOLIM1, golgin B1
External IDsOMIM: 602500; MGI: 1099447; HomoloGene: 68401; GeneCards: GOLGB1; OMA:GOLGB1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_030035

RefSeq (protein)

n/a

Location (UCSC)Chr 3: 121.66 – 121.75 MbChr 16: 36.7 – 36.75 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Giantin or Golgin subfamily B member 1 is a protein that in humans is encoded by the GOLGB1 gene.[5][6][7]

Structure

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Giantin is a disulfide-linked homodimer which contains several (around 37) coiled-coiled domains.

Function

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GOLGB1 protein has been shown to interact with ACBD3 and with PLK3[8] and vesicle tethering small GTPases Rab1 and Rab6.[9] Giantin also interacts with P115 at the N-terminal coils facilitating binding to the other Golgi matrix protein GM130[10] that is thought to be important for Golgi secretory function. Loss-of function studies of giantin have also suggested a role in primary cilia[11][12] function and defective regulation of glycosyltransferase expression and calcineurin signalling in tissue culture cells.[13][14]

Giantin is located at the cis-medial rims of the Golgi apparatus and is part of the Golgi matrix that is responsible for membrane trafficking in secretory pathway of proteins. This function is key for proper localisation of proteins at the plasma membrane and outside the cell (extracellular region) which is important for cell function that is dependent on for example receptors and the extracellular matrix function.

Clinical significance

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Recent animal model knockout studies of GOLGB1 in mice,[15] rat,[16] and zebrafish[11] have shown that phenotypes are different between species ranging from mild to severe craniofacial defects in the rodent models to just minor size defects in zebrafish. However, in adult zebrafish a tumoral calcinosis-like phenotype was observed, and in humans such phenotype has been linked to defective glycosyltransferase function (e.g. GALNT3 protein).[13]

References

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  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000173230 Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000034243 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. 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.
  6. 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.
  7. "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.
  8. 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.
  9. 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.
  10. 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.
  11. 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.
  12. 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.
  13. 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.
  14. 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.
  15. 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.
  16. 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

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