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J Biol Chem. 2011 May 13;286(19):16879-90. doi: 10.1074/jbc.M110.186932. Epub 2011 Mar 7.

AMP-activated protein kinase (AMPK) activation and glycogen synthase kinase-3β (GSK-3β) inhibition induce Ca2+-independent deposition of tight junction components at the plasma membrane.

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  • 1Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.

Abstract

Extracellular Ca(2+) is essential for the development of stable epithelial tight junctions. We find that in the absence of extracellular Ca(2+), AMP-activated protein kinase (AMPK) activation and glycogen synthase kinase (GSK)-3β inhibition independently induce the localization of epithelial tight junction components to the plasma membrane. The Ca(2+)-independent deposition of junctional proteins induced by AMPK activation and GSK-3β inhibition is independent of E-cadherin. Furthermore, the nectin-afadin system is required for the deposition of tight junction components induced by AMPK activation, but it is not required for that induced by GSK-3β inhibition. Phosphorylation studies demonstrate that afadin is a substrate for AMPK. These data demonstrate that two kinases involved in regulating cell growth and metabolism act through distinct pathways to influence the deposition of the components of epithelial tight junctions.

PMID:
21383016
PMCID:
PMC3089531
DOI:
10.1074/jbc.M110.186932
[PubMed - indexed for MEDLINE]
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