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Structural highlights

Disease

EGLN_HUMAN Heritable pulmonary arterial hypertension;Familial cerebral saccular aneurysm;Generalized juvenile polyposis/juvenile polyposis coli;Hereditary hemorrhagic telangiectasia. The disease is caused by variants affecting the gene represented in this entry.

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.EGLN_HUMAN Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis (PubMed:21737454, PubMed:23300529). Required for normal structure and integrity of adult vasculature (PubMed:7894484). Regulates the migration of vascular endothelial cells (PubMed:17540773). Required for normal extraembryonic angiogenesis and for embryonic heart development (By similarity). May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (By similarity). May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors (PubMed:1692830). Acts as a TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors (PubMed:21737454, PubMed:22347366, PubMed:23300529, PubMed:8370410). Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3 (PubMed:21737454, PubMed:22347366, PubMed:23300529).[UniProtKB:Q63961]^{[1] [2] [3] [4] [5] [6]}

See Also

• Growth differentiation factor 3D STRUCTURES

References

1. ↑ Lee NY, Blobe GC. The interaction of endoglin with beta-arrestin2 regulates transforming growth factor-beta-mediated ERK activation and migration in endothelial cells. J Biol Chem. 2007 Jul 20;282(29):21507-17. PMID:17540773 doi:10.1074/jbc.M700176200
2. ↑ Castonguay R, Werner ED, Matthews RG, Presman E, Mulivor AW, Solban N, Sako D, Pearsall RS, Underwood KW, Seehra J, Kumar R, Grinberg AV. Soluble endoglin specifically binds bone morphogenetic proteins 9 and 10 via its orphan domain, inhibits blood vessel formation, and suppresses tumor growth. J Biol Chem. 2011 Aug 26;286(34):30034-46. PMID:21737454 doi:10.1074/jbc.M111.260133
3. ↑ Nolan-Stevaux O, Zhong W, Culp S, Shaffer K, Hoover J, Wickramasinghe D, Ruefli-Brasse A. Endoglin requirement for BMP9 signaling in endothelial cells reveals new mechanism of action for selective anti-endoglin antibodies. PLoS One. 2012;7(12):e50920. doi: 10.1371/journal.pone.0050920. Epub 2012 Dec 27. PMID:23300529 doi:http://dx.doi.org/10.1371/journal.pone.0050920
4. ↑ McAllister KA, Grogg KM, Johnson DW, Gallione CJ, Baldwin MA, Jackson CE, Helmbold EA, Markel DS, McKinnon WC, Murrell J, et al.. Endoglin, a TGF-beta binding protein of endothelial cells, is the gene for hereditary haemorrhagic telangiectasia type 1. Nat Genet. 1994 Dec;8(4):345-51. PMID:7894484 doi:10.1038/ng1294-345
5. ↑ Bellón T, Corbí A, Lastres P, Calés C, Cebrián M, Vera S, Cheifetz S, Massague J, Letarte M, Bernabéu C. Identification and expression of two forms of the human transforming growth factor-beta-binding protein endoglin with distinct cytoplasmic regions. Eur J Immunol. 1993 Sep;23(9):2340-5. PMID:8370410 doi:10.1002/eji.1830230943
6. ↑ Gougos A, Letarte M. Primary structure of endoglin, an RGD-containing glycoprotein of human endothelial cells. J Biol Chem. 1990 May 25;265(15):8361-4 PMID:1692830
7. ↑ Saito T, Bokhove M, Croci R, Zamora-Caballero S, Han L, Letarte M, de Sanctis D, Jovine L. Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1. Cell Rep. 2017 May 30;19(9):1917-1928. doi: 10.1016/j.celrep.2017.05.011. PMID:28564608 doi:http://dx.doi.org/10.1016/j.celrep.2017.05.011