Cargando…
Structural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)
Protein O-glucosyltransferase 1/Rumi-mediated glucosylation of Notch epidermal growth factor-like (EGF-like) domains plays an important role in Notch signaling. Protein O-glucosyltransferase 1 shows specificity for folded EGF-like domains, it can only glycosylate serine residues in the C(1)XSXPC(2)...
Autores principales: | Li, Zhijie, Fischer, Michael, Satkunarajah, Malathy, Zhou, Dongxia, Withers, Stephen G., Rini, James M. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5543122/ https://www.ncbi.nlm.nih.gov/pubmed/28775322 http://dx.doi.org/10.1038/s41467-017-00255-7 |
Ejemplares similares
-
POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1
por: Williamson, Daniel B., et al.
Publicado: (2021) -
Protein O-Glucosyltransferase 1 (POGLUT1) Promotes Mouse Gastrulation through Modification of the Apical Polarity Protein CRUMBS2
por: Ramkumar, Nitya, et al.
Publicado: (2015) -
Xylosyl Extension of O-Glucose Glycans on the Extracellular Domain of NOTCH1 and NOTCH2 Regulates Notch Cell Surface Trafficking
por: Urata, Yusuke, et al.
Publicado: (2020) -
Glucosylation of (±)-Menthol by Uridine-Diphosphate-Sugar Dependent Glucosyltransferases from Plants
por: Kurze, Elisabeth, et al.
Publicado: (2021) -
Characterization of a Bifunctional O- and N-Glucosyltransferase from Vitis vinifera in Glucosylating Phenolic Compounds and 3,4-dichloroaniline in Pichia pastoris and Arabidopsis thaliana
por: Xu, Zhi-Sheng, et al.
Publicado: (2013)