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

Zhang, Lihong; Jouret, François; Rinehart, Jesse; Sfakianos, Jeff; Mellman, Ira; Lifton, Richard P.; Young, Lawrence H.; Caplan, Michael J.

doi:10.1074/jbc.m110.186932

Cited by 48 publications

(50 citation statements)

References 60 publications

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“…5A,B). As previously reported (Zhang et al, 2011), the addition of Ca 2+ to the culture medium induced the interaction between I-afadin and ZO-1. The co-immunoprecipitation of I-afadin and ZO-1 was significantly increased in the presence of the R-568 compound.…”

Section: +supporting

confidence: 48%

“…This manipulation is referred to as a 'Ca 2+ switch', and is associated with a rise of the cytosolic concentration of Ca 2+ (Cereijido et al, 1978;Gonzalez-Mariscal et al, 1990). Previous observations from our group and others have demonstrated that the Ca 2+ switch stimulates various independent cellular cascades, including the protein kinase C (PKC), the AMP-activated protein kinase (AMPK) and the glycogen synthase kinase 3b (GSK-3b) pathways (Balda et al, 1991;Zhang et al, 2006;Zheng and Cantley, 2007;Zhang et al, 2011). In MDCK cells, a Ca 2+ switch is typically associated with the activation of AMPK and the inhibition of GSK-3b.…”

Section: +mentioning

confidence: 99%

“…Activated AMPK phosphorylates I-afadin, at AJ sites, thereby inducing its interaction with and the recruitment of the TJ-associated protein ZO-1 to the plasma membrane. By contrast, I-afadin appears not to be required for the assembly of TJs caused by GSK-3b inhibition (Zhang et al, 2011).…”

Section: +mentioning

confidence: 99%

“…Furthermore, both Ca 2+ switch and AMPK activation increase the physical interaction between ZO-1 and I-afadin, a peripheral membrane protein located at the AJ that participates in organizing intercellular adhesive junctions (Ooshio et al, 2010;Zhang et al, 2011). Therefore, we assessed whether the relocation of ZO-1 to the plasma membrane following the activation of the CaSR involved the AMPK pathway.…”

Section: +mentioning

confidence: 99%

“…In MDCK cells, the formation of TJs requires the transient interaction of ZO-1 with I-afadin at the sites of initial cell-cell adhesions (Ooshio et al, 2010;Zhang et al, 2011). Thus, we tested whether the relocation of ZO-1 to the plasma membrane following the activation of CaSR involved such an interaction between ZO-1 and I-afadin.…”

Section: +mentioning

confidence: 99%

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Activation of the calcium-sensing receptor induces deposition of tight junction components to the epithelial cell plasma membrane

Jouret

Hull

et al. 2013

Journal of Cell Science

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SummaryThe Ca 2+ -sensing receptor (CaSR) belongs to the G-protein-coupled receptor superfamily and plays essential roles in divalent ion homeostasis and cell differentiation. Because extracellular Ca 2+ is essential for the development of stable epithelial tight junctions (TJs), we hypothesized that the CaSR participates in regulating TJ assembly. We first assessed the expression of the CaSR in Madin-Darby canine kidney (MDCK) cells at steady state and following manipulations that modulate TJ assembly. Next, we examined the effects of CaSR agonists and antagonists on TJ assembly. Immunofluorescence studies indicate that endogenous CaSR is located at the basolateral pole of MDCK cells. Stable transfection of human CaSR in MDCK cells further reveals that this protein co-distributes with b-catenin on the basolateral membrane. Switching MDCK cells from low-Ca 2+ medium to medium containing a normal Ca 2+ concentration significantly increases CaSR expression at both the mRNA and protein levels. Exposure of MDCK cells maintained in low-Ca 2+ conditions to the CaSR agonists neomycin, Gd 3+ or R-568 causes the transient relocation of the tight junction components ZO-1 and occludin to sites of cell-cell contact, while inducing no significant changes in the expression of mRNAs encoding junction-associated proteins. Stimulation of CaSR also increases the interaction between ZO-1 and the F-actin-binding protein I-afadin. This effect does not involve activation of the AMP-activated protein kinase. By contrast, CaSR inhibition by NPS-2143 significantly decreases interaction of ZO-1 with I-afadin and reduces deposition of ZO-1 at the cell surface following a Ca 2+ switch from 5 mM to 200 mM [Ca 2+ ] e . Pre-exposure of MDCK cells to the cell-permeant Ca 2+ chelator BAPTA-AM, similarly prevents TJ assembly caused by CaSR activation. Finally, stable transfection of MDCK cells with a cDNA encoding a human disease-associated gain-of-function mutant form of the CaSR increases the transepithelial electrical resistance of these cells in comparison to expression of the wild-type human CaSR. These observations suggest that the CaSR participates in regulating TJ assembly.

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Section: +supporting

confidence: 48%

Section: +mentioning

confidence: 99%

Section: +mentioning

confidence: 99%

Section: +mentioning

confidence: 99%

Section: +mentioning

confidence: 99%

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Activation of the calcium-sensing receptor induces deposition of tight junction components to the epithelial cell plasma membrane

Jouret

Hull

et al. 2013

Journal of Cell Science

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Cell Signalling During Blastocyst Morphogenesis

Eckert

Velazquez

Fleming

2015

Advances in Experimental Medicine and Biology

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Blastocyst morphogenesis is prepared for even before fertilisation. Information stored within parental gametes can influence both maternal and embryonic gene expression programmes after egg activation at fertilisation. A complex network of intrinsic, cell-cell mediated and extrinsic, embryo-environment signalling mechanisms operates throughout cleavage, compaction and cavitation. These signalling events not only ensure developmental progression, cell differentiation and lineage allocation to inner cell mass (embryo proper) and trophectoderm (future extraembryonic lineages) but also provide a degree of developmental plasticity ensuring survival in prevailing conditions by adaptive responses. Indeed, many cellular functions including differentiation, metabolism, gene expression and gene expression regulation are subject to plasticity with short- or long-term consequences even into adult life. The interplay between intrinsic and extrinsic signals impacting on blastocyst morphogenesis is becoming clearer. This has been best studied in the mouse which will be the focus of this chapter but translational significance to human and domestic animal embryology will be a focus in future years.

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Apaf1-deficient cortical neurons exhibit defects in axonal outgrowth

Zio

Molinari

Rizza

et al. 2015

Cell. Mol. Life Sci.

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The establishment of neuronal polarity and axonal outgrowth are key processes affecting neuronal migration and synapse formation, their impairment likely leading to cognitive deficits. Here we have found that the apoptotic protease activating factor 1 (Apaf1), apart from its canonical role in apoptosis, plays an additional function in cortical neurons, where its deficiency specifically impairs axonal growth. Given the central role played by centrosomes and microtubules in the polarized extension of the axon, our data suggest that Apaf1-deletion affects axonal outgrowth through an impairment of centrosome organization. In line with this, centrosomal protein expression, as well as their centrosomal localization proved to be altered upon Apaf1-deletion. Strikingly, we also found that Apaf1-loss affects trans-Golgi components and leads to a robust activation of AMP-dependent protein kinase (AMPK), this confirming the stressful conditions induced by Apaf1-deficiency. Since AMPK hyper-phosphorylation is known to impair a proper axon elongation, our finding contributes to explain the effect of Apaf1-deficiency on axogenesis. We also discovered that the signaling pathways mediating axonal growth and involving glycogen synthase kinase-3β, liver kinase B1, and collapsing-response mediator protein-2 are altered in Apaf1-KO neurons. Overall, our results reveal a novel non-apoptotic role for Apaf1 in axonal outgrowth, suggesting that the neuronal phenotype due to Apaf1-deletion could not only be fully ascribed to apoptosis inhibition, but might also be the result of defects in axogenesis. The discovery of new molecules involved in axonal elongation has a clinical relevance since it might help to explain neurological abnormalities occurring during early brain development.

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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

Cited by 48 publications

References 60 publications

Activation of the calcium-sensing receptor induces deposition of tight junction components to the epithelial cell plasma membrane

Activation of the calcium-sensing receptor induces deposition of tight junction components to the epithelial cell plasma membrane

Cell Signalling During Blastocyst Morphogenesis

Apaf1-deficient cortical neurons exhibit defects in axonal outgrowth

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