Deglycosylation of Na+/K+-ATPase causes the basolateral protein to undergo apical targeting in polarized hepatic cells

Wei Nan Lian, Tzu Wei Wu, Ro Lan Dao, Yann Jang Chen, Chi Hung Lin*

*Corresponding author for this work

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Polarized epithelia, such as hepatocytes, target their integral membrane proteins to specific apical or basolateral membrane domains during or after biogenesis. The roles played by protein glycosylation in this sorting process remain controversial. We report here that deglycosylation treatments in well-polarized hepatic cells by deglycosylation drugs, or by site-directed mutagenesis of the N-linked-glycosylation residues, all cause the Na+/K+-ATPase β-subunit to traffic from the native basolateral to the apical/ canalicular domain. Deglycosylated β-subunits are still able to bind and therefore transport the catalytic α-subunits to the aberrant apical location. Such apical targeting is mediated via the indirect transcytosis pathway. Cells containing apical Na+/K+-ATPase appear to be defective in maintaining the ionic gradient across the plasma membrane and in executing hepatic activities that are dependent upon the ionic homeostasis such as canalicular excretion.

Original languageEnglish
Pages (from-to)11-22
Number of pages12
JournalJournal of cell science
Volume119
Issue number1
DOIs
StatePublished - 1 Jan 2006

Keywords

  • Glycosylation
  • Liver
  • Na/K-ATPase
  • Protein targeting

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