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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ten Hagen, Kelly G. Van Dijk Härd, Iris Zhang, Liping Syed, Zulfeqhar Ali Lim, Jae-min Wells, Lance |
| Description | Author Affiliation: Zhang L ( Developmental Glycobiology Section, Laboratory of Cell and Developmental Biology, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892-4370); Syed ZA ( Department of Medical Genetics, Institute of Biomedicine.); van Dijk Härd I ( Institute of Health and Care Sciences, University of Gothenburg, SE-405 30 Gothenburg, Sweden); Lim JM ( Department of Chemistry, Changwon National University, Changwon, Gyeongnam 641-773, South Korea); Wells L ( Department of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602-4712.); Ten Hagen KG ( Developmental Glycobiology Section, Laboratory of Cell and Developmental Biology, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892-4370); |
| Abstract | Polarized secretion is crucial in many tissues. The conserved protein modification, O-glycosylation, plays a role in regulating secretion. However, the mechanisms by which this occurs are unknown. Here, we demonstrate that an O-glycosyltransferase functions as a novel regulator of secretion and secretory vesicle formation in vivo by glycosylating the essential Golgi/endoplasmic reticulum protein, Tango1 (Transport and Golgi organization 1), and conferring protection from furin-mediated proteolysis. Loss of the O-glycosyltransferase PGANT4 resulted in Tango1 cleavage, loss of secretory granules, and disrupted apical secretion. The secretory defects seen upon loss of pgant4 could be rescued either by overexpression of Tango1 or by knockdown of a specific furin (Dfur2) in vivo. Our studies elucidate a novel regulatory mechanism whereby secretion is influenced by the yin/yang of O-glycosylation and proteolytic cleavage. Moreover, our data have broader implications for the potential treatment of diseases resulting from the loss of O-glycosylation by modulating the activity of specific proteases. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 20 |
| Volume Number | 111 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2014-05-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Aryl Hydrocarbon Receptor Nuclear Translocator Metabolism Drosophila Proteins N-Acetylgalactosaminyltransferases Subtilisins Animals Calcinosis Catalysis Drosophila Melanogaster Endoplasmic Reticulum Glycosylation Golgi Apparatus Mucins Mutation Protein Binding Protein Processing, Post-Translational RNA Interference Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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