ArticleThe Journal of biological chemistry2011
A role for ZO-1 and PLEKHA7 in recruiting paracingulin to tight and adherens junctions of epithelial cells.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.
- Association of genetic variants with primary angle closure glaucoma in two different populations.PloS one · 2013Pooled it
- Translation efficiency covariation identifies conserved coordination patterns across cell types.Nature biotechnology · 2026Article
- Paracingulin controls the junctional accumulation of nonmuscle myosin-2 in endothelial cells in vivo.microPublication biology · 2025Article
- Paracingulin recruits CAMSAP3 to tight junctions and regulates microtubule and polarized epithelial cell organization.Journal of cell science · 2024Article
- Article
- Cingulin and paracingulin tether myosins-2 to junctions to mechanoregulate the plasma membrane.The Journal of cell biology · 2023Article
- Critical roles of adherens junctions in diseases of the oral mucosa.Tissue barriers · 2023Article
- The hTERT-p50 homodimer inhibits PLEKHA7 expression to promote gastric cancer invasion and metastasis.Oncogene · 2023Article
- Impact of rs11024102 PLEKHA7, rs3753841 COL11A1 single nucleotide polymorphisms, and serum levels of oxidative stress markers on the risk of primary angle-closure glaucoma in Egyptians.Journal, genetic engineering & biotechnology · 2022Article
- Cingulin binds to the ZU5 domain of scaffolding protein ZO-1 to promote its extended conformation, stabilization, and tight junction accumulation.The Journal of biological chemistry · 2022Article
- Origin and Evolution of the Multifaceted Adherens Junction Component Plekha7.Frontiers in cell and developmental biology · 2022Article
- PLEKHA5, PLEKHA6, and PLEKHA7 bind to PDZD11 to target the Menkes ATPase ATP7A to the cell periphery and regulate copper homeostasis.Molecular biology of the cell · 2021Article
- Updates on Genes and Genetic Mechanisms Implicated in Primary Angle-Closure Glaucoma.The application of clinical genetics · 2021Review
- WW, PH and C-Terminal Domains Cooperate to Direct the Subcellular Localizations of PLEKHA5, PLEKHA6 and PLEKHA7.Frontiers in cell and developmental biology · 2021Article
- Alveolar epithelial glycocalyx shedding aggravates the epithelial barrier and disrupts epithelial tight junctions in acute respiratory distress syndrome.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2021Article
- A Weak Link with Actin Organizes Tight Junctions to Control Epithelial Permeability.Developmental cell · 2020Article
- Cooperative binding of the tandem WW domains of PLEKHA7 to PDZD11 promotes conformation-dependent interaction with tetraspanin 33.The Journal of biological chemistry · 2020Article
- Tight Junctions in Cell Proliferation.International journal of molecular sciences · 2019Review
- The role of microtubules in the regulation of epithelial junctions.Tissue barriers · 2018Review
- Curcumin modulates chronic myelogenous leukemia exosomes composition and affects angiogenic phenotype via exosomal miR-21.Oncotarget · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 cadherin-based cell-cell junctions in Rat1 fibroblasts requires the ZIM-containing 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.