ArticleThe Journal of biological chemistry2009
Interaction of the RhoA exchange factor Net1 with discs large homolog 1 protects it from proteasome-mediated degradation and potentiates Net1 activity.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 35 citations in OpenAlex.
- MANCR lncRNA Modulates Cell-Cycle Progression and Metastasis by Cis-Regulation of NuclearMolecular and cellular biology · 2024Article
- Neuroepithelial cell-transforming 1 promotes cardiac fibrosis via the Wnt/β-catenin signaling pathway.iScience · 2023Article
- Src stimulates Abl-dependent phosphorylation of the guanine exchange factor Net1A to promote its cytosolic localization and cell motility.The Journal of biological chemistry · 2023Article
- Cdk1 phosphorylation negatively regulates the activity of Net1 towards RhoA during mitosis.Cellular signalling · 2021Article
- MotifAnalyzer-PDZ: A computational program to investigate the evolution of PDZ-binding target specificity.Protein science : a publication of the Protein Society · 2019Article
- Spatial Rho regulation: Molecular mechanisms controlling the GAP protein DLC3.Small GTPases · 2019Article
- Stress-activated MAPKs and CRM1 regulate the subcellular localization of Net1A to control cell motility and invasion.Journal of cell science · 2018Article
- Improved affinity at the cost of decreased specificity: a recurring theme in PDZ-peptide interactions.Scientific reports · 2016Article
- Regulating Rho GTPases and their regulators.Nature reviews. Molecular cell biology · 2016Review
- Regulation of RhoA activation and cytoskeletal organization by acetylation.Small GTPases · 2016Article
- Acetylation of the RhoA GEF Net1A controls its subcellular localization and activity.Journal of cell science · 2015Article
- Expression of polarity genes in human cancer.Cancer informatics · 2015Article
- The RhoGEF Net1 is required for normal mammary gland development.Molecular endocrinology (Baltimore, Md.) · 2014Article
- Regulation of focal adhesion kinase activation, breast cancer cell motility, and amoeboid invasion by the RhoA guanine nucleotide exchange factor Net1.Molecular and cellular biology · 2013Article
- Rac1 controls the subcellular localization of the Rho guanine nucleotide exchange factor Net1A to regulate focal adhesion formation and cell spreading.Molecular and cellular biology · 2013Article
- Article
- Neuroepithelial transforming gene 1 (Net1) binds to caspase activation and recruitment domain (CARD)- and membrane-associated guanylate kinase-like domain-containing (CARMA) proteins and regulates nuclear factor κB activation.The Journal of biological chemistry · 2012Article
- Timing is everything: Rac1 controls Net1A localization to regulate cell adhesion.Cell adhesion & migrationArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Net1 is a nuclear Rho guanine nucleotide exchange factor that is specific for the RhoA subfamily of small G proteins. Truncated forms of Net1 are transforming in NIH3T3 cells, and this activity requires cytoplasmic localization of Net1 as well as the presence of a COOH-terminal PDZ binding site. We have previously shown that Net1 interacts with PDZ domain-containing proteins within the Discs Large (Dlg) family and relocalizes them to the nucleus. In the present work, we demonstrate that Net1 binds directly to the first two PDZ domains of Dlg1 and that both PDZ domains are required for maximal interaction in cells. Furthermore, we show that Net1 is an unstable protein in MCF7 breast epithelial cells and that interaction with Dlg1 significantly enhances Net1 stability. Stabilization by Dlg1 significantly increases the ability of Net1 to stimulate RhoA activation in cells. The stability of endogenous Net1 is strongly enhanced by cell-cell contact, and this correlates with a dramatic increase in the interaction between Net1 and Dlg1. Importantly, disruption of E-cadherin-mediated cell contacts, either by depletion of external calcium or by treatment with transforming growth factor beta, leads to a rapid loss of the interaction between Net1 and Dlg1 and a subsequent increase in the ubiquitylation of Net1. These results indicate that Net1 requires interaction with PDZ domain proteins, such as Dlg1, to protect it from proteasome-mediated degradation and to maximally stimulate RhoA and that this interaction is regulated by cell-cell contact.
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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.