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Kato, K.* ; Jeanneau, C.* ; Tarp, M.A.* ; Benet-Pagès, A. ; Lorenz-Depiereux, B. ; Bennett, E.P.* ; Mandel, U.* ; Strom, T.M. ; Clausen, H.*

Polypeptide GaINAc-transferase T3 and familial tumoral calcinosis.

J. Biol. Chem. 281, 18370-18377 (2006)
DOI PMC
Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
Mutations in the gene encoding the glycosyltransferase polypeptide GalNAc-T3, which is involved in initiation of O-glycosylation, were recently identified as a cause of the rare autosomal recessive metabolic disorder familial tumoral calcinosis (OMIM 211900). Familial tumoral calcinosis is associated with hyperphosphatemia and massive ectopic calcifications. Here, we demonstrate that the secretion of the phosphaturic factor fibroblast growth factor 23 (FGF23) requires O-glycosylation, and that GalNAc-T3 selectively directs O-glycosylation in a subtilisin-like proprotein convertase recognition sequence motif, which blocks processing of FGF23. The study suggests a novel posttranslational regulatory model of FGF23 involving competing O-glycosylation and protease processing to produce intact FGF23.
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Publication type Article: Journal article
Document type Scientific Article
ISSN (print) / ISBN 0021-9258
e-ISSN 1083-351X
Journal Journal of Biological Chemistry, The
Quellenangaben Volume: 281, Issue: 27, Pages: 18370-18377 Article Number: , Supplement: ,
Publisher American Society for Biochemistry and Molecular Biology
Reviewing status Peer reviewed
Institute(s) Institute of Human Genetics (IHG)