ArticleThe Journal of cell biology2021
RhoGAP19D inhibits Cdc42 laterally to control epithelial cell shape and prevent invasion.
Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The trial behind it
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Systematic analysis of RhoGAP expression and function in border cell morphology and migration.bioRxiv : the preprint server for biology · 2026Article
- LGL-1 and the RhoGAP protein PAC-1 redundantly polarize thebioRxiv : the preprint server for biology · 2026Article
- Adherens junctions limit septate junction length in Drosophila midgut enterocytes but are not required for polarity.Journal of cell science · 2025Article
- A PAR6-aPKC-LGL structure reveals how LGL antagonizes aPKC.Nature structural & molecular biology · 2025Article
- Fas2EB112: a tale of two chromosomes.G3 (Bethesda, Md.) · 2024Article
- Article
- Systematic analysis of RhoGEF/GAP localizations uncovers regulators of mechanosensing and junction formation during epithelial cell division.Current biology : CB · 2023Article
- A bipartite, low-affinity roadblock domain-containing GAP complex regulates bacterial front-rear polarity.PLoS genetics · 2022Article
- Apical-basal polarity and the control of epithelial form and function.Nature reviews. Molecular cell biology · 2022Review
- Rho and Rab Family Small GTPases in the Regulation of Membrane Polarity in Epithelial Cells.Frontiers in cell and developmental biology · 2022Review
- MRCK: a master regulator of tissue remodeling or another 'ROCK' in the epithelial block?Tissue barriers · 2021Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 3 countries.
Funding
Abstract
Cdc42-GTP is required for apical domain formation in epithelial cells, where it recruits and activates the Par-6-aPKC polarity complex, but how the activity of Cdc42 itself is restricted apically is unclear. We used sequence analysis and 3D structural modeling to determine which Drosophila GTPase-activating proteins (GAPs) are likely to interact with Cdc42 and identified RhoGAP19D as the only high-probability Cdc42GAP required for polarity in the follicular epithelium. RhoGAP19D is recruited by α-catenin to lateral E-cadherin adhesion complexes, resulting in exclusion of active Cdc42 from the lateral domain. rhogap19d mutants therefore lead to lateral Cdc42 activity, which expands the apical domain through increased Par-6/aPKC activity and stimulates lateral contractility through the myosin light chain kinase, Genghis khan (MRCK). This causes buckling of the epithelium and invasion into the adjacent tissue, a phenotype resembling that of precancerous breast lesions. Thus, RhoGAP19D couples lateral cadherin adhesion to the apical localization of active Cdc42, thereby suppressing epithelial invasion.
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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 Socratic graph.