TGFBR3

TGFBR3
Identifiers
Aliases	TGFBR3, BGCAN, betaglycan, transforming growth factor beta receptor 3
External IDs	OMIM: 600742 MGI: 104637 HomoloGene: 2436 GeneCards: TGFBR3
Genetically Related Diseases
type 2 diabetes mellitus[1]
Gene ontology Molecular function • transforming growth factor beta receptor binding • heparin binding • activin binding • transforming growth factor beta receptor activity, type III • transforming growth factor beta-activated receptor activity • SMAD binding • PDZ domain binding • coreceptor activity • fibroblast growth factor binding • type II transforming growth factor beta receptor binding • protein binding • glycosaminoglycan binding • transforming growth factor beta binding Cellular component • extracellular exosome • extracellular region • cytoplasm • integral component of membrane • proteinaceous extracellular matrix • inhibin-betaglycan-ActRII complex • integral component of plasma membrane • membrane • cell surface • receptor complex • plasma membrane • external side of plasma membrane • extracellular fluid Biological process • response to hypoxia • heart trabecula formation • intracellular signal transduction • liver development • animal organ regeneration • definitive erythrocyte differentiation • BMP signaling pathway • negative regulation of cellular component movement • positive regulation of transforming growth factor beta receptor signaling pathway • regulation of protein binding • heart morphogenesis • transforming growth factor beta receptor complex assembly • cardiac epithelial to mesenchymal transition • pathway-restricted SMAD protein phosphorylation • response to follicle-stimulating hormone • ventricular cardiac muscle tissue morphogenesis • palate development • cardiac muscle cell proliferation • response to prostaglandin E • protein complex assembly • negative regulation of transforming growth factor beta receptor signaling pathway • negative regulation of epithelial cell proliferation • cell migration • definitive hemopoiesis • cell growth • epithelial to mesenchymal transition • response to luteinizing hormone • immune response • transforming growth factor beta receptor signaling pathway • epicardium-derived cardiac fibroblast cell development • ventricular septum morphogenesis • regulation of ERK1 and ERK2 cascade • ventricular compact myocardium morphogenesis • heart trabecula morphogenesis • positive regulation of cardiac muscle cell proliferation • regulation of JNK cascade • muscular septum morphogenesis • vasculogenesis involved in coronary vascular morphogenesis • outflow tract morphogenesis Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7049	21814
Ensembl	ENSG00000069702	ENSMUSG00000029287
UniProt	Q03167	O88393
RefSeq (mRNA)	NM_001195683 NM_001195684 NM_003243	NM_011578
RefSeq (protein)	NP_001182612.1 NP_001182613.1 NP_003234.2	NP_035708.2
Location (UCSC)	Chr 1: 91.68 – 91.91 Mb	Chr 5: 107.11 – 107.29 Mb
PubMed search	[2]	[3]
Wikidata

View/Edit Human

View/Edit Mouse

Betaglycan also known as Transforming growth factor beta receptor III (TGFBR3), is a cell-surface chondroitin sulfate / heparan sulfate proteoglycan >300 kDa in molecular weight. Betaglycan binds to various members of the TGF-beta superfamily of ligands via its core protein, and bFGF via its heparan sulfate chains. It is not involved directly in TGF-beta signal transduction but by binding to various member of the TGF-beta superfamily at the cell surface it acts as a reservoir of ligand for TGF-beta receptors.^[4][5]

See also

• TGF beta receptors

References

1. "Diseases that are genetically associated with TGFBR3 view/edit references on wikidata".
2. "Human PubMed Reference:".
3. "Mouse PubMed Reference:".
4. Andres JL, Stanley K, et al. (1989). "Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta". J. Cell Biol. 109 (6 (Pt 1)): 3137–3145. doi:10.1083/jcb.109.6.3137. PMC 2115961. PMID 2592419.
5. Andres JL, DeFalcis D, et al. (1992). "Binding of two growth factor families to separate domains of the proteoglycan betaglycan". J. Biol. Chem. 267 (9): 5927–5930. PMID 1556106.

Further reading

• Massagué J (1992). "Receptors for the TGF-beta family". Cell. 69 (7): 1067–70. doi:10.1016/0092-8674(92)90627-O. PMID 1319842.
• Border WA, Noble NA (1994). "Transforming growth factor beta in tissue fibrosis". N. Engl. J. Med. 331 (19): 1286–92. doi:10.1056/NEJM199411103311907. PMID 7935686.
• Morén A, Ichijo H, Miyazono K (1992). "Molecular cloning and characterization of the human and porcine transforming growth factor-beta type III receptors". Biochem. Biophys. Res. Commun. 189 (1): 356–62. doi:10.1016/0006-291X(92)91566-9. PMID 1333192.
• López-Casillas F, Cheifetz S, Doody J, et al. (1991). "Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system". Cell. 67 (4): 785–95. doi:10.1016/0092-8674(91)90073-8. PMID 1657406.
• Wang XF, Lin HY, Ng-Eaton E, et al. (1991). "Expression cloning and characterization of the TGF-beta type III receptor". Cell. 67 (4): 797–805. doi:10.1016/0092-8674(91)90074-9. PMID 1657407.
• Lin HY, Moustakas A, Knaus P, et al. (1995). "The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands". J. Biol. Chem. 270 (6): 2747–54. doi:10.1074/jbc.270.6.2747. PMID 7852346.
• López-Casillas F, Payne HM, Andres JL, Massagué J (1994). "Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites". J. Cell Biol. 124 (4): 557–68. doi:10.1083/jcb.124.4.557. PMC 2119924. PMID 8106553.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Johnson DW, Qumsiyeh M, Benkhalifa M, Marchuk DA (1996). "Assignment of human transforming growth factor-beta type I and type III receptor genes (TGFBR1 and TGFBR3) to 9q33-q34 and 1p32-p33, respectively". Genomics. 28 (2): 356–7. doi:10.1006/geno.1995.1157. PMID 8530052.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Brown CB, Boyer AS, Runyan RB, Barnett JV (1999). "Requirement of type III TGF-beta receptor for endocardial cell transformation in the heart". Science. 283 (5410): 2080–2. doi:10.1126/science.283.5410.2080. PMID 10092230.
• Gao J, Symons AL, Bartold PM (1999). "Expression of transforming growth factor-beta receptors types II and III within various cells in the rat periodontium". J. Periodont. Res. 34 (2): 113–22. doi:10.1111/j.1600-0765.1999.tb02230.x. PMID 10207840.
• Lewis KA, Gray PC, Blount AL, et al. (2000). "Betaglycan binds inhibin and can mediate functional antagonism of activin signalling". Nature. 404 (6776): 411–4. doi:10.1038/35006129. PMID 10746731.
• Zippert R, Bässler A, Holmer SR, et al. (2000). "Eleven single nucleotide polymorphisms and one triple nucleotide insertion of the human TGF-beta III receptor gene". J. Hum. Genet. 45 (4): 250–3. doi:10.1007/s100380070035. PMID 10944857.
• Rotzer D, Roth M, Lutz M, et al. (2001). "Type III TGF-β receptor-independent signalling of TGF-β2 via TβRII-B, an alternatively spliced TGF-β type II receptor". EMBO J. 20 (3): 480–90. doi:10.1093/emboj/20.3.480. PMC 133482. PMID 11157754.
• Blobe GC, Schiemann WP, Pepin MC, et al. (2001). "Functional roles for the cytoplasmic domain of the type III transforming growth factor beta receptor in regulating transforming growth factor beta signaling". J. Biol. Chem. 276 (27): 24627–37. doi:10.1074/jbc.M100188200. PMID 11323414.
• De Crescenzo G, Grothe S, Zwaagstra J, et al. (2001). "Real-time monitoring of the interactions of transforming growth factor-beta (TGF-beta ) isoforms with latency-associated protein and the ectodomains of the TGF-beta type II and III receptors reveals different kinetic models and stoichiometries of binding". J. Biol. Chem. 276 (32): 29632–43. doi:10.1074/jbc.M009765200. PMID 11382746.
• Blobe GC, Liu X, Fang SJ, et al. (2001). "A novel mechanism for regulating transforming growth factor beta (TGF-beta) signaling. Functional modulation of type III TGF-beta receptor expression through interaction with the PDZ domain protein, GIPC". J. Biol. Chem. 276 (43): 39608–17. doi:10.1074/jbc.M106831200. PMID 11546783.

External links

• betaglycan at the US National Library of Medicine Medical Subject Headings (MeSH)