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      C-mannosylation of R-spondin3 regulates its secretion and activity of Wnt/β-catenin signaling in cells

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          Abstract

          <p class="first" id="d12826415e115">R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis. In this study, we focused on C-mannosylation, a unique type of glycosylation, of human Rspo3. Rspo3 has two putative C-mannosylation sites at Trp(153) and Trp(156) ; however, it had been unclear whether these sites are C-mannosylated or not. We demonstrated that Rspo3 was C-mannosylated at both Trp(153) and Trp(156) by mass spectrometry. Using C-mannosylation-defective Rspo3 mutant-overexpressing cell lines, we found that C-mannosylation of Rspo3 promotes its secretion and activates Wnt/β-catenin signaling. </p>

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          Wnt signaling and cancer.

          Paul Polakis (2000)
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            Mechanisms of Wnt signaling in development.

            A Wodarz, R Nusse (1998)
            Wnt genes encode a large family of secreted, cysteine-rich proteins that play key roles as intercellular signaling molecules in development. Genetic studies in Drosophila and Caenorhabditis elegans, ectopic gene expression in Xenopus, and gene knockouts in the mouse have demonstrated the involvement of Wnts in processes as diverse as segmentation, CNS patterning, and control of asymmetric cell divisions. The transduction of Wnt signals between cells proceeds in a complex series of events including post-translational modification and secretion of Wnts, binding to transmembrane receptors, activation of cytoplasmic effectors, and, finally, transcriptional regulation of target genes. Over the past two years our understanding of Wnt signaling has been substantially improved by the identification of Frizzled proteins as cell surface receptors for Wnts and by the finding that beta-catenin, a component downstream of the receptor, can translocate to the nucleus and function as a transcriptional activator. Here we review recent data that have started to unravel the mechanisms of Wnt signaling.
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              LGR4 and LGR5 are R-spondin receptors mediating Wnt/β-catenin and Wnt/PCP signalling.

              Andrei Glinka, Christine Dolde, Nadine Kirsch … (2011)
              R-spondins are secreted Wnt signalling agonists, which regulate embryonic patterning and stem cell proliferation, but whose mechanism of action is poorly understood. Here we show that R-spondins bind to the orphan G-protein-coupled receptors LGR4 and LGR5 by their Furin domains. Gain- and loss-of-function experiments in mammalian cells and Xenopus embryos indicate that LGR4 and LGR5 promote R-spondin-mediated Wnt/β-catenin and Wnt/PCP signalling. R-spondin-triggered β-catenin signalling requires Clathrin, while Wnt3a-mediated β-catenin signalling requires Caveolin-mediated endocytosis, suggesting that internalization has a mechanistic role in R-spondin signalling.
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                Author and article information

                Journal
                Title: FEBS Letters
                Abbreviated Title: FEBS Lett
                Publisher: Wiley
                ISSN: 00145793
                Publication date Created: August 2016
                Publication date (Print): August 2016
                Publication date (Electronic): July 13 2016
                Volume: 590
                Issue: 16
                Pages: 2639-2649
                Affiliations
                [1 ]Department of Applied Chemistry; Faculty of Science and Technology; Keio University; Yokohama Japan
                [2 ]Biomolecular Characterization Unit; RIKEN Center for Sustainable Resource Science; Wako Japan
                Article
                DOI: 10.1002/1873-3468.12274
                PubMed ID: 27350215
                SO-VID: 0fcc0675-c0fd-43d8-a353-5800de9cc5e0
                Copyright © © 2016
                License:

                http://doi.wiley.com/10.1002/tdm_license_1.1

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