Nature Communications (Feb 2023)
Identification of global inhibitors of cellular glycosylation
- Daniel Madriz Sørensen,
- Christian Büll,
- Thomas D. Madsen,
- Erandi Lira-Navarrete,
- Thomas Mandel Clausen,
- Alex E. Clark,
- Aaron F. Garretson,
- Richard Karlsson,
- Johan F. A. Pijnenborg,
- Xin Yin,
- Rebecca L. Miller,
- Sumit K. Chanda,
- Thomas J. Boltje,
- Katrine T. Schjoldager,
- Sergey Y. Vakhrushev,
- Adnan Halim,
- Jeffrey D. Esko,
- Aaron F. Carlin,
- Ramon Hurtado-Guerrero,
- Roberto Weigert,
- Henrik Clausen,
- Yoshiki Narimatsu
Affiliations
- Daniel Madriz Sørensen
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Christian Büll
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Thomas D. Madsen
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Erandi Lira-Navarrete
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Thomas Mandel Clausen
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Alex E. Clark
- Department of Medicine, University of California, San Diego
- Aaron F. Garretson
- Department of Medicine, University of California, San Diego
- Richard Karlsson
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Johan F. A. Pijnenborg
- Institute for Molecules and Materials, Department of Synthetic Organic Chemistry, Radboud University Nijmegen
- Xin Yin
- Immunity and Pathogenesis Program, Infectious and Inflammatory Disease Center, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road
- Rebecca L. Miller
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Sumit K. Chanda
- Immunity and Pathogenesis Program, Infectious and Inflammatory Disease Center, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road
- Thomas J. Boltje
- Institute for Molecules and Materials, Department of Synthetic Organic Chemistry, Radboud University Nijmegen
- Katrine T. Schjoldager
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Sergey Y. Vakhrushev
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Adnan Halim
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Jeffrey D. Esko
- Department of Cellular and Molecular Medicine, University of California, San Diego
- Aaron F. Carlin
- Department of Cellular and Molecular Medicine, University of California, San Diego
- Ramon Hurtado-Guerrero
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Roberto Weigert
- Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health
- Henrik Clausen
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- Yoshiki Narimatsu
- Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen
- DOI
- https://doi.org/10.1038/s41467-023-36598-7
- Journal volume & issue
-
Vol. 14,
no. 1
pp. 1 – 19
Abstract
Here, the authors discover small molecules that inhibit glycosylation processes that occur in the Golgi apparatus of cells. The molecules reversibly inhibit formation of elaborate glycan structures without affecting secretion of glycoproteins.