University of Massachusetts Medical School Faculty Publications

Title

Molecular determinants of co- and post-translational N-glycosylation of type I transmembrane peptides

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Date

8-1-2013

Document Type

Article

Medical Subject Headings

Animals; CHO Cells; Cricetinae; Glycosylation; Hexosyltransferases; Membrane Proteins; Peptides; Potassium Channels, Voltage-Gated; Protein Processing, Post-Translational

Disciplines

Biochemistry | Molecular Biology

Abstract

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.

Rights and Permissions

Citation: Biochem J. 2013 Aug 1;453(3):427-34. doi: 10.1042/BJ20130028. Link to article on publisher's site

Related Resources

Link to Article in PubMed

PubMed ID

23718681