Structure of the human GlcNAc-1-phosphotransferase αβ subunits reveals regulatory mechanism for lysosomal enzyme glycan phosphorylation
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
https://www.nature.com/articles/s41594-022-00748-0.pdf
Reference37 articles.
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2. Burda, P. & Aebi, M. The dolichol pathway of N-linked glycosylation. Biochim. Biophys. Acta 1426, 239–257 (1999).
3. Bai, L. & Li, H. Cryo-EM is uncovering the mechanism of eukaryotic protein N-glycosylation. FEBS J. 286, 1638–1644 (2019).
4. Kudo, M. et al. The α- and β-subunits of the human UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase [corrected] are encoded by a single cDNA. J. Biol. Chem. 280, 36141–36149 (2005).
5. Raas-Rothschild, A. et al. Molecular basis of variant pseudo-Hurler polydystrophy (mucolipidosis IIIC). J. Clin. Invest. 105, 673–681 (2000).
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