Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3
نویسندگان
چکیده
منابع مشابه
MicroRNA-297a regulates vascular calcification by targeting fibroblast growth factor 23
Objective(s): Vascular calcification is one the major characteristics in patients with various types of chronic inflammatory disorders. MiRNAs have been shown to be involved in many normal biological functions as well as diseases; however, their role in vascular calcification has not received much attention. Materials and Methods: In the current study, we built a vascular calcification rat mode...
متن کاملHow fibroblast growth factor 23 works.
There is a discontinuum of hereditary and acquired disorders of phosphate homeostasis that are caused by either high or low circulating levels of the novel phosphaturic hormone fibroblastic growth factor 23 (FGF23). Disorders that are caused by high circulating levels of FGF23 are characterized by hypophosphatemia, decreased production of 1,25-dihydroxyvitamin D, and rickets/osteomalacia. On th...
متن کاملDynamic regulation of FGF23 by Fam20C phosphorylation, GalNAc-T3 glycosylation, and furin proteolysis.
The family with sequence similarity 20, member C (Fam20C) has recently been identified as the Golgi casein kinase. Fam20C phosphorylates secreted proteins on Ser-x-Glu/pSer motifs and loss-of-function mutations in the kinase cause Raine syndrome, an often-fatal osteosclerotic bone dysplasia. Fam20C is potentially an upstream regulator of the phosphate-regulating hormone fibroblast growth factor...
متن کاملmicrorna-297a regulates vascular calcification by targeting fibroblast growth factor 23
objective(s): vascular calcification is one the major characteristics in patients with various types of chronic inflammatory disorders. mirnas have been shown to be involved in many normal biological functions as well as diseases; however, their role in vascular calcification has not received much attention. materials and methods: in the current study, we built a vascular calcification rat mode...
متن کاملThe lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation.
Initiation of mucin-type O-glycosylation is controlled by a large family of UDP GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). Most GalNAc-transferases contain a ricin-like lectin domain in the C-terminal end, which may confer GalNAc-glycopeptide substrate specificity to the enzyme. We have previously shown that the lectin domain of GalNAc-T4 modulates its substrat...
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ژورنال
عنوان ژورنال: Nature Chemical Biology
سال: 2020
ISSN: 1552-4450,1552-4469
DOI: 10.1038/s41589-019-0444-x