ArticleJournal of cell science2019
The Rho family GEF FARP2 is activated by aPKCι to control tight junction formation and polarity.
Article in Journal of cell science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Article
- PARD6A promotes lung adenocarcinoma cell proliferation and invasion through Serpina3.Cancer gene therapy · 2024Article
- Into the fold: advances in understanding aPKC membrane dynamics.The Biochemical journal · 2023Article
- Control of atypical PKCι membrane dissociation by tyrosine phosphorylation within a PB1-C1 interdomain interface.The Journal of biological chemistry · 2023Article
- Comparative transcriptome analysis provides insight into the molecular targets and signaling pathways of deer TGF-1 regulating chondrocytes proliferation and differentiation.Molecular biology reports · 2023Article
- Separable mechanisms drive local and global polarity establishment in the Caenorhabditiselegans intestinal epithelium.Development (Cambridge, England) · 2022Article
- A Scribble/Cdep/Rac pathway controls follower-cell crawling and cluster cohesion during collective border-cell migration.Developmental cell · 2022Article
- Rho and Rab Family Small GTPases in the Regulation of Membrane Polarity in Epithelial Cells.Frontiers in cell and developmental biology · 2022Review
- Rac-GEF/Rac Signaling and Metastatic Dissemination in Lung Cancer.Frontiers in cell and developmental biology · 2020Article
- Autoactivation of small GTPases by the GEF-effector positive feedback modules.F1000Research · 2019Review
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
The elaboration of polarity is central to organismal development and to the maintenance of functional epithelia. Among the controls determining polarity are the PAR proteins, PAR6, aPKCι and PAR3, regulating both known and unknown effectors. Here, we identify FARP2 as a 'RIPR' motif-dependent partner and substrate of aPKCι that is required for efficient polarisation and junction formation. Binding is conferred by a FERM/FA domain-kinase domain interaction and detachment promoted by aPKCι-dependent phosphorylation. FARP2 is shown to promote GTP loading of Cdc42, which is consistent with it being involved in upstream regulation of the polarising PAR6-aPKCι complex. However, we show that aPKCι acts to promote the localised activity of FARP2 through phosphorylation. We conclude that this aPKCι-FARP2 complex formation acts as a positive feedback control to drive polarisation through aPKCι and other Cdc42 effectors.This article has an associated First Person interview with the first author of the paper.
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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.