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See detailMechanisms involved in AMPK-mediated deposition of tight junction components to the plasma membrane.
Wu, Jingshing; Rowart, Pascal; Jouret, François ULiege et al

in American journal of physiology. Cell physiology (2020)

AMP activated protein kinase (AMPK) activation promotes early stages of epithelial junction assembly. AMPK activation in MDCK renal epithelial cells facilitates localization of the junction-associated ... [more ▼]

AMP activated protein kinase (AMPK) activation promotes early stages of epithelial junction assembly. AMPK activation in MDCK renal epithelial cells facilitates localization of the junction-associated proteins aPKCzeta and Par3 to the plasma membrane and promotes conversion of Cdc42, a key regulator of epithelial polarization and junction assembly, to its active GTP bound state. Furthermore, Par3 is an important regulator of AMPK-mediated aPKCzeta localization. Both aPKCzeta and Par3 serve as intermediates in AMPK-mediated junction assembly, with inhibition of aPKCzeta activity or Par3 knockdown disrupting AMPK's ability to facilitate zonula occludens (ZO-1) localization. AMPK phosphorylates the adherens junction protein afadin and regulates its interaction with the tight junction protein zonula occludens (ZO)-1. Afadin is phosphorylated at two critical sites, S182 (residing within an aPKCzeta consensus site) and S1049 (residing within an AMPK consensus site), that are differentially regulated during junction assembly and that exert different effects on the process. Expression of phospho-defective mutants (S182A and S1082A) perturbed ZO-1 localization to the plasma membrane during AMPK-induced junction assembly. Expression of S182A increased the ZO-1/afadin interaction, while S1049A reduced this interaction during extracellular calcium-induced junction assembly. Inhibition of aPKCzeta activity also increased the ZO-1/afadin interaction. Taken together, these data suggest that aPKCzeta phosphorylation of afadin terminates the ZO-1/afadin interaction, and thus permits the later stages of junction assembly. [less ▲]

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See detailAMP-activated protein kinase (AMPK) activation and glycogen synthase kinase-3beta (GSK-3beta) inhibition induce Ca2+-independent deposition of tight junction components at the plasma membrane.
Zhang, Lihong ULiege; JOURET, François ULiege; Rinehart, Jesse et al

in Journal of Biological Chemistry (2011), 286(19), 16879-90

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 ... [more ▼]

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)-3beta 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-3beta 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-3beta 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. [less ▲]

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