ArticleMolecular and cellular biology2011
The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed, 58 citations in OpenAlex.
- Identification of PKN2 and MOB4 as Coordinators of Collective Cell Migration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Lysophosphatidic acid and sphingosine-1-phosphate are apical polarity cues in multiple organoid systems.Cell reports · 2025Article
- Illuminating understudied kinases: a generalizable biosensor development method applied to protein kinase N.Communications biology · 2025Article
- Role of PATJ in stroke prognosis by modulating endothelial to mesenchymal transition through the Hippo/Notch/PI3K axis.Cell death discovery · 2024Article
- Comparative Transcriptome Analysis of Spleen Reveals Potential Regulation of Genes and Immune Pathways Following Administration of Aeromonas salmonicida subsp. masoucida Vaccine in Atlantic Salmon (Salmo salar).Marine biotechnology (New York, N.Y.) · 2022Article
- PKN2 is involved in aggregation and spheroid formation of fibroblasts in suspension culture by regulating cell motility andBiochemistry and biophysics reports · 2021Article
- The structure and function of protein kinase C-related kinases (PRKs).Biochemical Society transactions · 2021Review
- Increasing the resolution and precision of psychiatric genome-wide association studies by re-imputing summary statistics using a large, diverse reference panel.American journal of medical genetics. Part B, Neuropsychiatric genetics : the official publication of the International Society of Psychiatric Genetics · 2021Review
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- Phosphorylation Sites in Protein Kinases and Phosphatases Regulated by Formyl Peptide Receptor 2 Signaling.International journal of molecular sciences · 2020Review
- Article
- Deducing the presence of proteins and proteoforms in quantitative proteomics.Nature communications · 2018Article
- The TORC2-Dependent Signaling Network in the Yeast Saccharomyces cerevisiae.Biomolecules · 2017Review
- A CDC42-centered signaling unit is a dominant positive regulator of endothelial integrity.Scientific reports · 2017Article
- Impaired lymphocyte trafficking in mice deficient in the kinase activity of PKN1.Scientific reports · 2017Article
- Diverse roles of guanine nucleotide exchange factors in regulating collective cell migration.The Journal of cell biology · 2017Article
- Cigarette Smoking-Associated Alterations in Serotonin/Adrenalin Signaling Pathways of Platelets.Journal of the American Heart Association · 2017Article
- PKN2 and Cdo interact to activate AKT and promote myoblast differentiation.Cell death & disease · 2016Article
- PKN3 is the major regulator of angiogenesis and tumor metastasis in mice.Scientific reports · 2016Article
- STAR syndrome-associated CDK10/Cyclin M regulates actin network architecture and ciliogenesis.Cell cycle (Georgetown, Tex.) · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Rho GTPases regulate multiple signaling pathways to control a number of cellular processes during epithelial morphogenesis. To investigate the downstream pathways through which Rho regulates epithelial apical junction formation, we screened a small interfering RNA (siRNA) library targeting 28 known Rho target proteins in 16HBE human bronchial epithelial cells. This led to the identification of the serine-threonine kinase PRK2 (protein kinase C-related kinase 2, also called PKN2). Depletion of PRK2 does not block the initial formation of primordial junctions at nascent cell-cell contacts but does prevent their maturation into apical junctions. PRK2 is recruited to primordial junctions, and this localization depends on its C2-like domain. Rho binding is essential for PRK2 function and also facilitates PRK2 recruitment to junctions. Kinase-dead PRK2 acts as a dominant-negative mutant and prevents apical junction formation. We conclude that PRK2 is recruited to nascent cell-cell contacts through its C2-like and Rho-binding domains and promotes junctional maturation through a kinase-dependent pathway.
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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.