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- Title
Polypeptide N-acetylgalactosamine transferase 3: a post-translational writer on human health.
- Authors
Garay, Yohana Camila; Cejas, Romina Beatriz; Lorenz, Virginia; Zlocowski, Natacha; Parodi, Pedro; Ferrero, Franco Alejandro; Angeloni, Genaro; García, Valentina Alfonso; Sendra, Victor German; Lardone, Ricardo Dante; Irazoqui, Fernando José
- Abstract
Polypeptide N-acetylgalactosamine transferase 3 (ppGalNAc-T3) is an enzyme involved in the initiation of O-GalNAc glycan biosynthesis. Acting as a writer of frequent post-translational modification (PTM) on human proteins, ppGalNAc-T3 has key functions in the homeostasis of human cells and tissues. We review the relevant roles of this molecule in the biosynthesis of O-GalNAc glycans, as well as in biological functions related to human physiological and pathological conditions. With main emphasis in ppGalNAc-T3, we draw attention to the different ways involved in the modulation of ppGalNAc-Ts enzymatic activity. In addition, we take notice on recent reports of ppGalNAc-T3 having different subcellular localizations, highlight critical intrinsic and extrinsic functions in cellular physiology that are exerted by ppGalNAc-T3-synthesized PTMs, and provide an update on several human pathologies associated with dysfunctional ppGalNAc-T3. Finally, we propose biotechnological tools as new therapeutic options for the treatment of pathologies related to altered ppGalNAc-T3. Key messages: ppGalNAc-T3 is a key enzyme in the human O-GalNAc glycans biosynthesis. enzyme activity is regulated by PTMs, lectin domain and protein–protein interactions. ppGalNAc-T3 is located in human Golgi apparatus and cell nucleus. ppGalNAc-T3 has a central role in cell physiology as well as in several pathologies. Biotechnological tools for pathological management are proposed.
- Subjects
GOLGI apparatus; POST-translational modification; CELL physiology; CELL nuclei; PROTEIN-protein interactions; GLYCANS
- Publication
Journal of Molecular Medicine, 2022, Vol 100, Issue 10, p1387
- ISSN
0946-2716
- Publication type
Article
- DOI
10.1007/s00109-022-02249-5