The Kv1.2 potassium channel: The position of an N-glycan on the extracellular linkers affects its protein expression and function

Jing Zhu, Esperanza Recio-Pinto, Torsten Hartwig, Will Sellers, Jingyi Yan, William B. Thornhill

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Voltage-gated potassium Kv1 channels have three extracellular linkers, the S1-S2, the S3-S4, and the S5-P. The S1-S2 is the only linker that has an N-glycan and it is at a conserved position on this linker on Kv1.1-Kv1.5 and Kv1.7 channels. We hypothesize that an N-glycan is found at only this position due to its effect on folding, trafficking, and/or function of these channels. To investigate this hypothesis, N-glycosylation sites were engineered at different positions on the extracellular linkers of Kv1.2 to determine the effects of N-glycans on channel surface protein expression and function. Our data suggest that for Kv1 channels, (1) placing an N-glycan at non-native positions on the S1-S2 linker decreased cell surface protein expression but the N-glycan still affected function similarly as if it were at its native position, (2) placing a non-native N-glycan on the S3-S4 linker significantly altered function, and (3) placing a non-native N-glycan on the S5-P linker disrupted both trafficking and function. We suggest that Kv1 channels have an N-glycan at a conserved position on only the S1-S2 linker to overcome the constraints for proper folding, trafficking, and function that appear to occur if the N-glycan is moved from this position.

Original languageEnglish (US)
Pages (from-to)16-29
Number of pages14
JournalBrain research
Volume1251
DOIs
StatePublished - Jan 28 2009
Externally publishedYes

Keywords

  • Activation
  • N-glycans
  • Potassium channel
  • Protein stability
  • Trafficking

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Clinical Neurology
  • Developmental Biology

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