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The Activation of Arylsulfatases

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The Activation of Arylsulfatases The activation of arylsulfatases D'Eustachio, P., Jassal, B. European Bioinformatics Institute, New York University Langone Medical Center, Ontario Institute for Cancer Research, Oregon Health and Science University. The contents of this document may be freely copied and distributed in any media, provided the authors, plus the institutions, are credited, as stated under the terms of Creative Commons Attribution 4.0 Inter- national (CC BY 4.0) License. For more information see our license. 04/06/2019 Introduction Reactome is open-source, open access, manually curated and peer-reviewed pathway database. Pathway annotations are authored by expert biologists, in collaboration with Reactome editorial staff and cross- referenced to many bioinformatics databases. A system of evidence tracking ensures that all assertions are backed up by the primary literature. Reactome is used by clinicians, geneticists, genomics research- ers, and molecular biologists to interpret the results of high-throughput experimental studies, by bioin- formaticians seeking to develop novel algorithms for mining knowledge from genomic studies, and by systems biologists building predictive models of normal and disease variant pathways. The development of Reactome is supported by grants from the US National Institutes of Health (P41 HG003751), University of Toronto (CFREF Medicine by Design), European Union (EU STRP, EMI-CD), and the European Molecular Biology Laboratory (EBI Industry program). Literature references Fabregat, A., Sidiropoulos, K., Viteri, G., Forner, O., Marin-Garcia, P., Arnau, V. et al. (2017). Reactome pathway ana- lysis: a high-performance in-memory approach. BMC bioinformatics, 18, 142. ↗ Sidiropoulos, K., Viteri, G., Sevilla, C., Jupe, S., Webber, M., Orlic-Milacic, M. et al. (2017). Reactome enhanced path- way visualization. Bioinformatics, 33, 3461-3467. ↗ Fabregat, A., Jupe, S., Matthews, L., Sidiropoulos, K., Gillespie, M., Garapati, P. et al. (2018). The Reactome Pathway Knowledgebase. Nucleic Acids Res, 46, D649-D655. ↗ Fabregat, A., Korninger, F., Viteri, G., Sidiropoulos, K., Marin-Garcia, P., Ping, P. et al. (2018). Reactome graph data- base: Efficient access to complex pathway data. PLoS computational biology, 14, e1005968. ↗ Reactome database release: 68 This document contains 1 pathway and 2 reactions (see Table of Contents) https://reactome.org Page 1 The activation of arylsulfatases ↗ Stable identifier: R-HSA-1663150 Sulfatase activity requires a unique posttranslational modification (PTM) of a catalytic cysteine residue into a formylglycine. This modification is impaired in patients with multiple sulfatase deficiency (MSD) due to defects in the SUMF1 (sulfatase-modifying factor 1) gene responsible for this PTM. SUMF2 can in- hibit the activity of SUMF1 thereby providing a mechanism for the regulation of sulfatase activation (Ghosh 2007, Diez-Roux & Ballabio 2005). Literature references Ghosh, D. (2007). Human sulfatases: a structural perspective to catalysis. Cell Mol Life Sci, 64, 2013-22. ↗ Diez-Roux, G., Ballabio, A. (2005). Sulfatases and human disease. Annu Rev Genomics Hum Genet, 6, 355-79. ↗ Editions 2011-10-14 Authored, Edited Jassal, B. 2012-05-15 Reviewed D'Eustachio, P. https://reactome.org Page 2 SUMF1 mediates the oxidation of cysteine to formylglycine, producing active aryl- sulfatases ↗ Location: The activation of arylsulfatases Stable identifier: R-HSA-1614362 Type: transition Compartments: endoplasmic reticulum lumen The sulfatase-modifying factor 1 (SUMF1, also called C-alpha-formylglycine-generating enzyme, FGE) (Preusser-Kunze et al. 2005, Cosma et al. 2003, Landgrebe et al. 2003) oxidises the critical cysteine residue in arylsulfatases to an active site 3-oxoalanine residue thus confering sulfatase activity (Roeser et al. 2006). Defects in SUMF1 cause multiple sulfatase deficiency (MSD) (MIM:272200), an impairment of aryl- sulfatase activity due to defective post-translational modification of the cysteine residue (Cosma et al. 2003, Dierks et al, 2003). This post-translational modification is thought to be highly conserved in euka- ryotes (Selmer et al. 1996, von Figura et al. 1998). SUMF1 is active as either a monomer or a homodimer. A monomer is described in this reaction. Literature references Preusser-Kunze, A., Mariappan, M., Schmidt, B., Gande, SL., Mutenda, K., Wenzel, D. et al. (2005). Molecular charac- terization of the human Calpha-formylglycine-generating enzyme. J Biol Chem, 280, 14900-10. ↗ Cosma, MP., Pepe, S., Annunziata, I., Newbold, RF., Grompe, M., Parenti, G. et al. (2003). The multiple sulfatase defi- ciency gene encodes an essential and limiting factor for the activity of sulfatases. Cell, 113, 445-56. ↗ Landgrebe, J., Dierks, T., Schmidt, B., von Figura, K. (2003). The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes. Gene, 316, 47-56. ↗ Dierks, T., Schmidt, B., Borissenko, LV., Peng, J., Preusser, A., Mariappan, M. et al. (2003). Multiple sulfatase defi- ciency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme. Cell, 113, 435-44. ↗ Selmer, T., Hallmann, A., Schmidt, B., Sumper, M., von Figura, K. (1996). The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri. Eur J Biochem, 238, 341-5. ↗ https://reactome.org Page 3 Editions 2011-09-28 Authored, Edited Jassal, B. 2012-05-15 Reviewed D'Eustachio, P. https://reactome.org Page 4 SUMF2 binds SUMF1, inhibiting SUMF1-mediated activation of arylsulfatases ↗ Location: The activation of arylsulfatases Stable identifier: R-HSA-1614336 Type: binding Compartments: endoplasmic reticulum lumen Sulfatase-modifying factor 2 (SUMF2, also called C-alpha-formylglycine-generating enzyme 2, pFGE) is the paralogue of SUMF1. While SUMF1 can modify a critical residue on arylsulfatases to confer activity to them, SUMF2 lacks this ability (Mariappan et al. 2005) and instead, SUMF2 can inhibit the action of SUMF1 by dimerising with it (Zito et al. 2005). SUMF2 can interact with sulfatases with and without SUMF1 (Zito et al. 2005). Literature references Mariappan, M., Preusser-Kunze, A., Balleininger, M., Eiselt, N., Schmidt, B., Gande, SL. et al. (2005). Expression, loc- alization, structural, and functional characterization of pFGE, the paralog of the Calpha-formylglycine-generat- ing enzyme. J Biol Chem, 280, 15173-9. ↗ Zito, E., Fraldi, A., Pepe, S., Annunziata, I., Kobinger, G., Di Natale, P. et al. (2005). Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2. EMBO Rep, 6, 655-60. ↗ Editions 2011-09-28 Authored, Edited Jassal, B. 2012-05-15 Reviewed D'Eustachio, P. https://reactome.org Page 5 Table of Contents Introduction 1 The activation of arylsulfatases 2 SUMF1 mediates the oxidation of cysteine to formylglycine, producing active arylsulfatases 3 SUMF2 binds SUMF1, inhibiting SUMF1-mediated activation of arylsulfatases 5 Table of Contents 6 https://reactome.org Page 6.
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