JNK is a novel regulator of intercellular adhesion

You, Hui; Lei, Pedro; Andreadis, Stelios T.

doi:10.4161/tisb.26845

Cited by 34 publications

(23 citation statements)

References 127 publications

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“…This strongly suggests that AJ and TJ disassembly represents a specific consequence of anillin depletion, which is independent of defective cytokinesis. Our findings fittingly agree with the emerging role of JNK in the regulation of epithelial junctions [58, 62]. Thus, many environmental stimuli are known to disrupt AJ and TJ integrity via JNK activation, whereas inhibition of JNK signaling promotes junctional assembly and enhances epithelial barriers in vitro and in vivo [59, 77-80].…”

Section: Discussionsupporting

confidence: 89%

“…Specifically, we investigated the roles of mitogen activated protein kinases (MAPK), which are modulated by signaling inputs from different cellular organelles, and are known regulators of epithelial junctions [57-62]. Immunoblotting analysis was used to compare the expression of three major MAPK, namely c-Jun N-terminal protein kinase (JNK), extracellular signal responsive/regulated kinases (ERK) 1/2, and p38 kinase in control and anillin-depleted DU145 cells.…”

Section: Resultsmentioning

confidence: 99%

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F-actin binding protein, anillin, regulates integrity of intercellular junctions in human epithelial cells

Wang

Chadha

Feygin

et al. 2015

Cell. Mol. Life Sci.

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Tight junctions (TJ) and adherens junctions (AJ) are key morphological features of differentiated epithelial cells that regulate the integrity and permeability of tissue barriers. Structure and remodeling of epithelial junctions depends on their association with the underlying actomyosin cytoskeleton. Anillin is a unique scaffolding protein interacting with different cytoskeletal components, including actin filaments and myosin motors. Its role in the regulation of mammalian epithelial junctions remains unexplored. Downregulation of anillin expression in human prostate, colonic, and lung epithelial cells triggered AJ and TJ disassembly without altering the expression of junctional proteins. This junctional disassembly was accompanied by dramatic disorganization of the perijunctional actomyosin belt; while the general architecture of the actin cytoskeleton, and activation status of non-muscle myosin II, remained unchanged. Furthermore, loss of anillin disrupted the adducin-spectrin membrane skeleton at the areas of cell-cell contact, selectively decreased γ-adducin expression, and induced cytoplasmic aggregation of αII-spectrin. Anillin knockdown activated c-Jun N-terminal kinase (JNK), and JNK inhibition restored AJ and TJ integrity and cytoskeletal organization in anillin-depleted cells. These findings suggest a novel role for anillin in regulating intercellular adhesion in model human epithelia by mechanisms involving the suppression of JNK activity and controlling the assembly of the perijunctional cytoskeleton.

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Section: Discussionsupporting

confidence: 89%

Section: Resultsmentioning

confidence: 99%

F-actin binding protein, anillin, regulates integrity of intercellular junctions in human epithelial cells

Wang

Chadha

Feygin

et al. 2015

Cell. Mol. Life Sci.

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“…Epithelial tissue organization is determined by specific epithelial cell-cell adhesion contacts that also serve important roles in cellular communication [10,11]. Amongst these, adherens junctions connect intercellular adhesion to the actin cytoskeleton and thus are crucial not only during morphogenesis of epithelial tissues but also in tissue homeostasis.…”

Section: Introductionmentioning

confidence: 99%

Pathological implications of cadherin zonation in mouse liver

Hempel

Schmitz

Winkler

et al. 2015

Cell. Mol. Life Sci.

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Both acute and chronic liver diseases are associated with ample re-modeling of the liver parenchyma leading to functional impairment, which is thus obviously the cause or the consequence of the disruption of the epithelial integrity. It was, therefore, the aim of this study to investigate the distribution of the adherens junction components E- and N-cadherin, which are important determinants of tissue cohesion. E-cadherin was expressed in periportal but not in perivenous hepatocytes. In contrast, N-cadherin was more enriched towards the perivenous hepatocytes. In agreement, β-catenin, which links both cadherins via α-catenin to the actin cytoskeleton, was expressed ubiquitously. This zonal expression of cadherins was preserved in acute liver injury after treatment with acetaminophen or partial hepatectomy, but disrupted in chronic liver damage like in non-alcoholic steatohepatitis (NASH) or α1-antitrypsin deficiency. Hepatocyte proliferation during acetaminophen-induced liver damage was predominant at the boundary between the damaged perivenous and the intact periportal parenchyma indicating a minor contribution of periportal hepatocytes to liver regeneration. In NASH livers, an oval cell reaction was observed pointing to massive tissue damage coinciding with the gross impairment of hepatocyte proliferation. In the liver parenchyma, metabolic functions are distributed heterogeneously. For example, the expression of phosphoenolpyruvate carboxykinase and E-cadherin overlapped in periportal hepatocytes. Thus, during liver regeneration after acute damage, the intact periportal parenchyma might sustain essential metabolic support like glucose supply or ammonia detoxification. However, disruption of epithelial integrity during chronic challenges may increase susceptibility to metabolic liver diseases such as NASH or vice versa. This might suggest the regulatory integration of tissue cohesion and metabolic functions in the liver.

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“…The further study on evaluating apoptotic proteins levels of BAX and Bcl-2 arrived at the consistent conclusion. JNK/MAPK signal pathway play crucial roles in tumor cell apoptosis (Meng et al, 2012;You et al, 2013;Bloch et al, 2014). p-JNK levels of KLF4 overexpression cells, curcumin treated cells and co-treated cells were notable less than the control.…”

Section: Discussionmentioning

confidence: 94%