ArticleThe Biochemical journal2009
Regulation of Rnd3 localization and function by protein kinase C alpha-mediated phosphorylation.
Article in The Biochemical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
45 citing papers in PubMed, 60 citations in OpenAlex.
- Review
- RND3 Enhances Cardiac Glucose Metabolism Through Inhibiting ACAT1-Dependent PDHA1 Acetylation and Protects Against Ischemia-Reperfusion Injury.Circulation · 2026Article
- Therapeutic targeting of post-translational modifications in ovarian cancer: mechanisms and clinical applications.Journal of ovarian research · 2025Review
- New insights on the regulators and inhibitors of RhoA-ROCK signalling in Parkinson's disease.Metabolic brain disease · 2025Review
- Molecular basis and current insights of atypical Rho small GTPase in cancer.Molecular biology reports · 2024Review
- Rnd3 Expression is Necessary to Maintain Mitochondrial Homeostasis but Dispensable for Autophagy.Frontiers in cell and developmental biology · 2022Article
- Different phosphorylation and farnesylation patterns tune Rnd3-14-3-3 interaction in distinct mechanisms.Chemical science · 2021Article
- Identification and characterization of a new isoform of small GTPase RhoE.Communications biology · 2020Article
- Dysregulation of Rho GTPases in Human Cancers.Cancers · 2020Review
- Inferring Novel Tumor Suppressor Genes with a Protein-Protein Interaction Network and Network Diffusion Algorithms.Molecular therapy. Methods & clinical development · 2018Article
- Lipid packing defects and membrane charge control RAB GTPase recruitment.Traffic (Copenhagen, Denmark) · 2018Article
- Rnd3-induced cell rounding requires interaction with Plexin-B2.Journal of cell science · 2016Article
- Rho GTPases: Regulation and roles in cancer cell biology.Small GTPases · 2016Review
- Regulating Rho GTPases and their regulators.Nature reviews. Molecular cell biology · 2016Review
- Rnd3 as a Novel Target to Ameliorate Microvascular Leakage.Journal of the American Heart Association · 2016Article
- Pathophysiological Functions of Rnd3/RhoE.Comprehensive Physiology · 2015Review
- RhoE is required for contact inhibition and negatively regulates tumor initiation and progression.Oncotarget · 2015Article
- Inference of Low and High-Grade Glioma Gene Regulatory Networks Delineates the Role of Rnd3 in Establishing Multiple Hallmarks of Cancer.PLoS genetics · 2015Article
- PKCα promotes the mesenchymal to amoeboid transition and increases cancer cell invasiveness.BMC cancer · 2015Article
- Signaling pathways that control rho kinase activity maintain the embryonic epicardial progenitor state.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
The Rnd proteins (Rnd1, Rnd2 and Rnd3/RhoE) form a distinct branch of the Rho family of small GTPases. Altered Rnd3 expression causes changes in cytoskeletal organization and cell cycle progression. Rnd3 functions to decrease RhoA activity, but how Rnd3 itself is regulated to cause these changes is still under investigation. Unlike other Rho family proteins, Rnd3 is regulated not by GTP/GDP cycling, but at the level of expression and by post-translational modifications such as prenylation and phosphorylation. We show in the present study that, upon PKC (protein kinase C) agonist stimulation, Rnd3 undergoes an electrophoretic mobility shift and its subcellular localization becomes enriched at internal membranes. These changes are blocked by inhibition of conventional PKC isoforms and do not occur in PKCalpha-null cells or to a non-phosphorylatable mutant of Rnd3. We further show that PKCalpha directly phosphorylates Rnd3 in an in vitro kinase assay. Additionally, we provide evidence that the phosphorylation status of Rnd3 has a direct effect on its ability to block signalling from the Rho-ROCK (Rho-kinase) pathway. These results identify an additional mechanism of regulation and provide clarification of how Rnd3 modulates Rho signalling to alter cytoskeletal organization.
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What OpenQuestion holds
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.