Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.

  title={Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.},
  author={Michael F. Beers and Ming Zhao and Yaniv Tomer and Scott J. Russo and Peggy Zhang and Linda W. Gonzales and Susan H. Guttentag and Surafel Mulugeta},
  journal={American journal of physiology. Lung cellular and molecular physiology},
  volume={305 12},
  • M. Beers, Ming Zhao, S. Mulugeta
  • Published 15 December 2013
  • Biology
  • American journal of physiology. Lung cellular and molecular physiology
The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis. The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140. A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle. To understand its role in… 

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