Molecular determinants of co- and post-translational N-glycosylation of type I transmembrane peptides
Department of Biochemistry and Molecular Pharmacology
Animals; CHO Cells; Cricetinae; Glycosylation; Hexosyltransferases; Membrane Proteins; Peptides; Potassium Channels, Voltage-Gated; Protein Processing, Post-Translational
Biochemistry | Molecular Biology
Type I transmembrane peptides acquire N-linked glycans during and after protein synthesis to facilitate anterograde trafficking through the secretory pathway. Mutations in N-glycosylation consensus sites (NXT and NXS, where X not equalP) that alter the kinetics of the initial N-glycan attachment have been associated with cardiac arrhythmias; however, the molecular determinants that define co- and post-translational consensus sites in proteins are not known. In the present study, we identified co- and post-translational consensus sites in the KCNE family of K+ channel regulatory subunits to uncover three determinants that favour co-translational N-glycosylation kinetics of type I transmembrane peptides which lack a cleavable signal sequence: threonine-containing consensus sites (NXT), multiple N-terminal consensus sites and long C-termini. The identification of these three molecular determinants now makes it possible to predict co- and post-translational consensus sites in type I transmembrane peptides.
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Citation: Biochem J. 2013 Aug 1;453(3):427-34. doi: 10.1042/BJ20130028. Link to article on publisher's site
The Biochemical journal
Malaby, Heidi and Kobertz, William R., "Molecular determinants of co- and post-translational N-glycosylation of type I transmembrane peptides" (2013). University of Massachusetts Medical School Faculty Publications. 532.