ArticleMolecular and cellular biology2011
The Ras inhibitors caveolin-1 and docking protein 1 activate peroxisome proliferator-activated receptor γ through spatial relocalization at helix 7 of its ligand-binding domain.
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 27 papers.
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Who cites it
27 citing papers in PubMed, 39 citations in OpenAlex.
- Nuclear pore protein POM121 regulates subcellular localization and transcriptional activity of PPARγ.Cell death & disease · 2024Article
- Ha-RasBiomedicines · 2022Article
- PPARγ induces PD-L1 expression in MSS+ colorectal cancer cells.Oncoimmunology · 2021Article
- Myotubularin-related protein 7 activates peroxisome proliferator-activated receptor-gamma.Oncogenesis · 2020Article
- EphB1 interaction with caveolin-1 in endothelial cells modulates caveolae biogenesis.Molecular biology of the cell · 2020Article
- Article
- EHD2 regulates adipocyte function and is enriched at cell surface-associated lipid droplets in primary human adipocytes.Molecular biology of the cell · 2019Article
- Article
- Cell-free formation and interactome analysis of caveolae.The Journal of cell biology · 2018Article
- Epigenetic silencing of tumor suppressor candidate 3 confers adverse prognosis in early colorectal cancer.Oncotarget · 2017Article
- Caveolin-1: An Oxidative Stress-Related Target for Cancer Prevention.Oxidative medicine and cellular longevity · 2017Review
- Deficient Adipogenesis of Scleroderma Patient and Healthy African American Monocytes.Frontiers in pharmacology · 2017Article
- Article
- Inhibition of Rho-Associated Kinase 1/2 Attenuates Tumor Growth in Murine Gastric Cancer.Neoplasia (New York, N.Y.) · 2016Article
- Subcellular compartmentalization of docking protein-1 contributes to progression in colorectal cancer.EBioMedicine · 2016Article
- Caveolin-1 regulates cancer cell metabolism via scavenging Nrf2 and suppressing MnSOD-driven glycolysis.Oncotarget · 2016Article
- Peroxisome Proliferator-Activated Receptor γ-Mediated Inhibition on Hypoxia-Triggered Store-Operated Calcium Entry. A Caveolin-1-Dependent Mechanism.American journal of respiratory cell and molecular biology · 2015Article
- Tagging strategies strongly affect the fate of overexpressed caveolin-1.Traffic (Copenhagen, Denmark) · 2015Article
- Caveolin-1 deficiency induces a MEK-ERK1/2-Snail-1-dependent epithelial-mesenchymal transition and fibrosis during peritoneal dialysis.EMBO molecular medicine · 2015Article
- Minireview: Challenges and opportunities in development of PPAR agonists.Molecular endocrinology (Baltimore, Md.) · 2014Review
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Authors and funding
12 authors at 8 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peroxisome proliferator-activated receptor γ (PPARγ) is a transcription factor that promotes differentiation and cell survival in the stomach. PPARγ upregulates and interacts with caveolin-1 (Cav1), a scaffold protein of Ras/mitogen-activated protein kinases (MAPKs). The cytoplasmic-to-nuclear localization of PPARγ is altered in gastric cancer (GC) patients, suggesting a so-far-unknown role for Cav1 in spatial regulation of PPARγ signaling. We show here that loss of Cav1 accelerated proliferation of normal stomach and GC cells in vitro and in vivo. Downregulation of Cav1 increased Ras/MAPK-dependent phosphorylation of serine 84 in PPARγ and enhanced nuclear translocation and ligand-independent transcription of PPARγ target genes. In contrast, Cav1 overexpression sequestered PPARγ in the cytosol through interaction of the Cav1 scaffolding domain (CSD) with a conserved hydrophobic motif in helix 7 of PPARγ's ligand-binding domain. Cav1 cooperated with the endogenous Ras/MAPK inhibitor docking protein 1 (Dok1) to promote the ligand-dependent transcriptional activity of PPARγ and to inhibit cell proliferation. Ligand-activated PPARγ also reduced tumor growth and upregulated the Ras/MAPK inhibitors Cav1 and Dok1 in a murine model of GC. These results suggest a novel mechanism of PPARγ regulation by which Ras/MAPK inhibitors act as scaffold proteins that sequester and sensitize PPARγ to ligands, limiting proliferation of gastric epithelial cells.
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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.