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Voss, Matthias; Künzel, Ulrike; Higel, Fabian; Kuhn, Peer‐Hendrik; Colombo, Alessio; Fukumori, Akio; Haug‐Kröper, Martina; Klier, Bärbel; Grammer, Gudula; Seidl, Andreas; Schröder, Bernd; Obst, Reinhard; Steiner, Harald; Lichtenthaler, Stefan F; Haass, Christian; Fluhrer, Regina

Shedding of glycan‐modifying enzymes by signal peptide peptidase‐like 3 (SPPL3) regulates cellular N‐glycosylation

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  • Medientyp: E-Artikel
  • Titel: Shedding of glycan‐modifying enzymes by signal peptide peptidase‐like 3 (SPPL3) regulates cellular N‐glycosylation
  • Beteiligte: Voss, Matthias; Künzel, Ulrike; Higel, Fabian; Kuhn, Peer‐Hendrik; Colombo, Alessio; Fukumori, Akio; Haug‐Kröper, Martina; Klier, Bärbel; Grammer, Gudula; Seidl, Andreas; Schröder, Bernd; Obst, Reinhard; Steiner, Harald; Lichtenthaler, Stefan F; Haass, Christian; Fluhrer, Regina
  • Erschienen: Springer Science and Business Media LLC, 2014
  • Erschienen in: The EMBO Journal
  • Sprache: Englisch
  • DOI: 10.15252/embj.201488375
  • ISSN: 0261-4189; 1460-2075
  • Schlagwörter: General Immunology and Microbiology ; General Biochemistry, Genetics and Molecular Biology ; Molecular Biology ; General Neuroscience
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  • Beschreibung: <jats:title>Abstract</jats:title><jats:p>Protein N‐glycosylation is involved in a variety of physiological and pathophysiological processes such as autoimmunity, tumour progression and metastasis. Signal peptide peptidase‐like 3 (<jats:styled-content style="fixed-case">SPPL</jats:styled-content>3) is an intramembrane‐cleaving aspartyl protease of the Gx<jats:styled-content style="fixed-case">GD</jats:styled-content> type. Its physiological function, however, has remained enigmatic, since presently no physiological substrates have been identified. We demonstrate that <jats:styled-content style="fixed-case">SPPL</jats:styled-content>3 alters the pattern of cellular N‐glycosylation by triggering the proteolytic release of active site‐containing ectodomains of glycosidases and glycosyltransferases such as N‐acetylglucosaminyltransferase V, β‐1,3 N‐acetylglucosaminyltransferase 1 and β‐1,4 galactosyltransferase 1. Cleavage of these enzymes leads to a reduction in their cellular activity. In line with that, reduced expression of <jats:styled-content style="fixed-case">SPPL</jats:styled-content>3 results in a hyperglycosylation phenotype, whereas elevated <jats:styled-content style="fixed-case">SPPL</jats:styled-content>3 expression causes hypoglycosylation. Thus, <jats:styled-content style="fixed-case">SPPL</jats:styled-content>3 plays a central role in an evolutionary highly conserved post‐translational process in eukaryotes.</jats:p>
  • Zugangsstatus: Freier Zugang