Involvement of the Interaction of Afadin with ZO-1 in the Formation of Tight Junctions in Madin-Darby Canine Kidney Cells

Ooshio, Takako; Kobayashi, Reiko; Ikeda, Wataru; Miyata, Muneaki; Fukumoto, Yuri; Matsuzawa, Naomi; Ogita, Hisakazu; Takai, Yoshimi

doi:10.1074/jbc.m109.043760

Cited by 117 publications

(135 citation statements)

References 47 publications

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“…In contrast, depletion of either ZO-1 or ZO-2 did not affect the junctional localization of AJ markers, such as p120ctn, afadin, and PLEKHA7 (supplemental Fig. 1B) and E-cadherin (data not shown), in agreement with the notion that ZO-1 specifically controls the assembly and function of TJ, but not AJ (13,42). Thus, ZO-1 is required for the efficient junctional recruitment of cingulin and, to a lesser extent, paracingulin.…”

Section: Paracingulin Interacts With Zo-1 Through the Zim-containing supporting

confidence: 74%

A Role for ZO-1 and PLEKHA7 in Recruiting Paracingulin to Tight and Adherens Junctions of Epithelial Cells

Pulimeno

Paschoud

Citi

2011

Journal of Biological Chemistry

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Paracingulin is a 160-kDa protein localized in the cytoplasmic region of epithelial tight and adherens junctions, where it regulates RhoA and Rac1 activities by interacting with guanine nucleotide exchange factors. Here, we investigate the molecular mechanisms that control the recruitment of paracingulin to cell-cell junctions. We show that paracingulin forms a complex with the tight junction protein ZO-1, and the globular head domain of paracingulin interacts directly with ZO-1 through an N-terminal region containing a conserved ZIM (ZO-1-Interaction-Motif) sequence. Recruitment of paracingulin to cadherinbased cell-cell junctions in Rat1 fibroblasts requires the ZIMcontaining region, whereas in epithelial cells removal of this region decreases the junctional localization of paracingulin at tight junctions but not at adherens junctions. Depletion of ZO-1, but not ZO-2, reduces paracingulin accumulation at tight junctions. A yeast two-hybrid screen identifies both ZO-1 and the adherens junction protein PLEKHA7 as paracingulin-binding proteins. Paracingulin forms a complex with PLEKHA7 and its interacting partner p120ctn, and the globular head domain of paracingulin interacts directly with a central region of PLEKHA7. Depletion of PLEKHA7 from Madin-Darby canine kidney cells results in the loss of junctional localization of paracingulin and a decrease in its expression. In summary, we characterize ZO-1 and PLEKHA7 as paracingulin-interacting proteins that are involved in its recruitment to epithelial tight and adherens junctions, respectively. Tight junctions (TJ)2 and adherens junctions (AJ) are key elements of the apical junctional complex of vertebrate epithelial cells and are of fundamental importance in the morphogenesis and homeostasis of epithelial tissues. TJ and AJ carry out several functions: canonical roles in cell-cell adhesion and tissue sorting (AJ), cell polarization and permeability barrier functions (TJ), and signaling functions through pathways that control the organization of the cytoskeleton and the activity of transcription factors (for review, see Refs.

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Section: Paracingulin Interacts With Zo-1 Through the Zim-containing supporting

confidence: 74%

A Role for ZO-1 and PLEKHA7 in Recruiting Paracingulin to Tight and Adherens Junctions of Epithelial Cells

Pulimeno

Paschoud

Citi

2011

Journal of Biological Chemistry

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“…We also included other genes known to be constitutively associated with TJ proteins and considered to be involved in the assembly and function of TJ, i.e., symplekin, 33) members of the aPKC/Par3/Par6 complex (Prkci, Prkcz, Pard3, Pard6a, Pard6b and Pard6g), Crb3/ Pals1/Patj complex (Crb3, Mpp5 and Inadl) 16) and afadin. 34) Among these genes, claudin-1, 4, 10 and occludin showed relatively high log ratios (0.36, 0.35, 0.54, and 0.35, respectively). The respective mean log ratios for the set of 30 genes at 0 d and 2 d were 0.02 and 0.14.…”

Section: Microarray Results and Differences Of Mean Expression Ratiosmentioning

confidence: 99%

“…We have included afadin in this study as one of the TJ-related genes, because it directly binds to ZO-1 before the formation of TJ and is involved in the first step of recruitment for TJ on the apical side of the cells. 34) Afadin is also essential to the formation of the adherens junction (AJ), and the formation of AJ is known to facilitate the assembly of TJ. 16) Genes related to AJ formation such as those encoding cadherins, catenins and nectins may therefore also be involved in the promotion of barrier recovery by dietary GC.…”

Section: Discussionmentioning

confidence: 99%

Orally Administered Glucosylceramide Improves the Skin Barrier Function by Upregulating Genes Associated with the Tight Junction and Cornified Envelope Formation

Ideta¹,

Sakuta²,

Nakano³

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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“…Afadin was a high-ranking hit in our EphA2 BioID screen (2D, #3; 3D, #13). In addition to its role as a cytoskeleton-junction linker, afadin has been implicated in tight junction regulation (Yamamoto et al, 1997;Ooshio et al, 2010;Monteiro et al, 2013;Choi et al, 2016;Mandai et al, 1997). We found that loss of afadin in NHEKs disrupted organization and function of tight junctions (Fig.…”

Section: Epha2 and Afadin Interact In Keratinocytesmentioning

confidence: 68%

“…Afadin is an actin-binding protein associated with nectin and cadherin-based adherens junctions, as well as tight junctions (Yamamoto et al, 1997;Ooshio et al, 2010;Mandai et al, 1997;Indra et al, 2014;Choi et al, 2016;Monteiro et al, 2013). Afadin was a high-ranking hit in our EphA2 BioID screen (2D, #3; 3D, #13).…”

Section: Epha2 and Afadin Interact In Keratinocytesmentioning

confidence: 99%

EphA2 proteomics in human keratinocytes reveals a novel association with afadin and epidermal tight junctions

White

Ventrella

Kaplan

et al. 2016

Journal of Cell Science

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EphA2 is a receptor tyrosine kinase that helps to maintain epidermal tissue homeostasis. A proximity-dependent biotin identification (BioID) approach was used to identify proteins in close proximity to EphA2 within primary human keratinocytes and three-dimensional (3D) reconstituted human epidermis (RHE) cultures to map a putative protein interaction network for this membrane receptor that exhibits a polarized distribution in stratified epithelia. Although a subset of known EphA2 interactors were identified in the BioID screen, >97% were uniquely detected in keratinocytes with over 50% of these vicinal proteins only present in 3D human epidermal culture. Afadin (AFDN), a cytoskeletal and junction-associated protein, was present in 2D and 3D keratinocyte cultures, and validated as a so-far-unknown EphA2-interacting protein. Loss of EphA2 protein disrupted the subcellular distribution of afadin and occludin in differentiated keratinocytes, leading to impairment of tight junctions. Collectively, these studies illustrate the use of the BioID approach in order to map receptor interaction networks in 3D human epithelial cultures, and reveal a positive regulatory role for EphA2 in the organization of afadin and epidermal tight junctions.

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Involvement of the Interaction of Afadin with ZO-1 in the Formation of Tight Junctions in Madin-Darby Canine Kidney Cells

Cited by 117 publications

References 47 publications

A Role for ZO-1 and PLEKHA7 in Recruiting Paracingulin to Tight and Adherens Junctions of Epithelial Cells

A Role for ZO-1 and PLEKHA7 in Recruiting Paracingulin to Tight and Adherens Junctions of Epithelial Cells

Orally Administered Glucosylceramide Improves the Skin Barrier Function by Upregulating Genes Associated with the Tight Junction and Cornified Envelope Formation

EphA2 proteomics in human keratinocytes reveals a novel association with afadin and epidermal tight junctions

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