Physiologic and pathophysiologic consequences of altered sialylation and glycosylation on ion channel function

Deniz Baycin-Hizal, Allan Gottschalk, Elena Jacobson, Sunny Mai, Daniel Wolozny, Hui Zhang, Sharon S. Krag, Michael J. Betenbaugh

Research output: Contribution to journalReview article

Abstract

Voltage-gated ion channels are transmembrane proteins that regulate electrical excitability in cells and are essential components of the electrically active tissues of nerves, muscle and the heart. Potassium channels are one of the largest subfamilies of voltage sensitive channels and are among the most-studied of the voltage-gated ion channels. Voltage-gated channels can be glycosylated and changes in the glycosylation pattern can affect ion channel function, leading to neurological and neuromuscular disorders and congenital disorders of glycosylation (CDG). Alterations in glycosylation can also be acquired and appear to play a role in development and aging. Recent studies have focused on the impact of glycosylation and sialylation on ion channels, particularly for voltage-gated potassium and sodium channels. The terminal step of sialylation often affects channel activation and inactivation kinetics. The presence of sialic acids on O or N-glycans can alter the gating mechanism and cause conformational changes in the voltage-sensing domains due to sialic acid's negative charges. This manuscript will provide an overview of sialic acids, potassium and sodium channel function, and the impact of sialylation on channel activation and deactivation.

Original languageEnglish (US)
Pages (from-to)243-253
Number of pages11
JournalBiochemical and Biophysical Research Communications
Volume453
Issue number2
DOIs
StatePublished - Oct 17 2014

Keywords

  • Congenital disorders of glycosylation
  • Glycosylation
  • Neurological disorders
  • Sialylation
  • Voltage-gated potassium channels
  • Voltage-gated sodium channels

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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