期刊
EMBO JOURNAL
卷 33, 期 24, 页码 2890-2905出版社
WILEY
DOI: 10.15252/embj.201488375
关键词
glycosyltransferases; GxGD aspartyl proteases; protein glycosylation; signal peptide peptidase like-3
资金
- Deutsche Forschungsgemeinschaft [IIA 1737-11, FL 635/2-1]
- Center for Integrated Protein Science Munich (CIPSM)
- European Research Council under the European Union's Seventh Framework Program (FP7)/ERC [321366-Amyloid]
- PhD fellowship of the Hans und Ilse Breuer Stiftung
- Elitenetwork of Bavaria within the Graduate Program Protein Dynamics in Health and Disease
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 (SPPL3) is an intramembrane-cleaving aspartyl protease of the GxGD type. Its physiological function, however, has remained enigmatic, since presently no physiological substrates have been identified. We demonstrate that SPPL3 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, beta-1,3 N-acetylglucosaminyltransferase 1 and beta-1,4 galactosyltransferase 1. Cleavage of these enzymes leads to a reduction in their cellular activity. In line with that, reduced expression of SPPL3 results in a hyperglycosylation phenotype, whereas elevated SPPL3 expression causes hypoglycosylation. Thus, SPPL3 plays a central role in an evolutionary highly conserved post-translational process in eukaryotes.
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