C. elegans DPY-19 Is a C-Mannosyltransferase Glycosylating Thrombospondin Repeats

Buettner, Falk F. R. and Ashikov, Angel and Tiemann, Birgit and Lehle, Ludwig and Bakker, Hans (2013) C. elegans DPY-19 Is a C-Mannosyltransferase Glycosylating Thrombospondin Repeats. MOLECULAR CELL, 50 (2). pp. 295-302. ISSN 1097-2765,

Full text not available from this repository. (Request a copy)

Abstract

Among the different types of protein glycosylation, C-mannosylation of tryptophan residues stands out because of the unique linkage formed between sugar and protein. Instead of the typical O- or N-glycosidic linkage, a C-C bond is used for attachment of a single mannose. C-mannose is characteristically found in thrombospondin type 1 repeats and in the WSXWS motif of type I cytokine receptors. The genetic base of the enzymatic activity catalyzing C-mannosylation was not known. Here we demonstrate that Caenorhabditis elegans DPY-19 is a C-mannosyltransferase. DPY-19 exhibits topological and sequential homology to the N-glycan oligosaccharyltransferase, highlighting an evolutionary link between N- and C-glycosylation. We show that the C. elegans surface receptors MIG-21 and UNC-5 are acceptor substrates of DPY-19 and that C-mannosylation is essential for the secretion of soluble MIG-21. Thereby, our data provide an explanation for the previously described identical Q neuroblast migration phenotypes of dpy-19 and mig-21 mutants.

Item Type: Article
Uncontrolled Keywords: PROTEIN O-MANNOSYLTRANSFERASES; STIMULATING FACTOR-RECEPTOR; RNASE U-S; WSXWS MOTIF; ERYTHROPOIETIN RECEPTOR; LIGAND-BINDING; EXTRACELLULAR DOMAIN; CYTOKINE RECEPTORS; PROLACTIN RECEPTOR; CRYSTAL-STRUCTURE;
Subjects: 500 Science > 580 Botanical sciences
Divisions: Biology, Preclinical Medicine > Institut für Pflanzenwissenschaften > Lehrstuhl für Zellbiologie und Pflanzenphysiologie (Prof. Dr. Klaus Grasser)
Depositing User: Dr. Gernot Deinzer
Date Deposited: 16 Apr 2020 08:01
Last Modified: 16 Apr 2020 08:01
URI: https://pred.uni-regensburg.de/id/eprint/16802

Actions (login required)

View Item View Item