Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease.

@article{Bas2011PosttranslationalNO,
  title={Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease.},
  author={Tuba Bas and Grace Y Gao and Anatoli Lvov and Kshama D Chandrasekhar and Reid Gilmore and William R Kobertz},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 32},
  pages={28150-9}
}
N-Glycosylation of membrane proteins is critical for their proper folding, co-assembly and subsequent matriculation through the secretory pathway. Here, we examine the kinetics of N-glycan addition to type I transmembrane KCNE1 K(+) channel β-subunits, where point mutations that prevent N-glycosylation at one consensus site give rise to disorders of the cardiac rhythm and congenital deafness. We show that KCNE1 has two distinct N-glycosylation sites: a typical co-translational site and a… CONTINUE READING
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