Journal
JOURNAL OF CELL SCIENCE
Volume 119, Issue 1, Pages 11-22Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.02706
Keywords
glycosylation. protein targeting; Na+/K+-ATPase; liver
Categories
Ask authors/readers for more resources
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 P-subunit to traffic from the native basolateral to the apical/canalicular domain. Deglycosylated beta-subunits are still able to bind and therefore transport the catalytic alpha-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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available