ArticleMolecular biology of the cell2006
CNF1-induced ubiquitylation and proteasome destruction of activated RhoA is impaired in Smurf1-/- cells.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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Who cites it
29 citing papers in PubMed, 1 synthesis or guideline pooled it, 59 citations in OpenAlex.
- Effects of theInternational journal of molecular sciences · 2021Pooled it
- An Anti-Invasive Role for Mdmx through the RhoA GTPase under the Control of the NEDD8 Pathway.Cells · 2024Article
- BAG6 supports stress fiber formation by preventing the ubiquitin-mediated degradation of RhoA.Molecular biology of the cell · 2023Article
- Smurf1 regulates ameloblast polarization by ubiquitination-mediated degradation of RhoA.Cell proliferation · 2023Article
- The Cytotoxic Necrotizing Factors (CNFs)-A Family of Rho GTPase-Activating Bacterial Exotoxins.Toxins · 2021Review
- SMURF1, a promoter of tumor cell progression?Cancer gene therapy · 2021Review
- Exploring the Roles of HERC2 and the NEDD4L HECT E3 Ubiquitin Ligase Subfamily in p53 Signaling and the DNA Damage Response.Frontiers in oncology · 2021Review
- Identification of cancer-associated missense mutations in hace1 that impair cell growth control and Rac1 ubiquitylation.Scientific reports · 2017Article
- Clathrin regulates lymphocyte migration by driving actin accumulation at the cellular leading edge.European journal of immunology · 2016Article
- PDR-1/hParkin negatively regulates the phagocytosis of apoptotic cell corpses in Caenorhabditis elegans.Cell death & disease · 2014Article
- Review
- Article
- The Rho family member RhoE interacts with Skp2 and is degraded at the proteasome during cell cycle progression.The Journal of biological chemistry · 2013Article
- The cytotoxic necrotizing factor 1 from E. coli: a janus toxin playing with cancer regulators.Toxins · 2013Review
- Article
- The GTPase-deficient Rnd proteins are stabilized by their effectors.The Journal of biological chemistry · 2012Article
- Cell cycle regulation of Rho signaling pathways.Cell cycle (Georgetown, Tex.) · 2012Review
- Prenylation of Rho G-proteins: a novel mechanism regulating gene expression and protein stability in human trabecular meshwork cells.Molecular neurobiology · 2012Article
- Rac1 acts in conjunction with Nedd4 and dishevelled-1 to promote maturation of cell-cell contacts.Journal of cell science · 2012Article
- Ubiquitination: Added complexity in Ras and Rho family GTPase function.Small GTPases · 2011Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Ubiquitylation of RhoA has emerged as an important aspect of both the virulence of Escherichia coli producing cytotoxic necrotizing factor (CNF) 1 toxin and the establishment of the polarity of eukaryotic cells. Owing to the molecular activity of CNF1, we have investigated the relationship between permanent activation of RhoA catalyzed by CNF1 and subsequent ubiquitylation of RhoA by Smurf1. Using Smurf1-deficient cells and by RNA interference (RNAi)-mediated Smurf1 knockdown, we demonstrate that Smurf1 is a rate-limiting and specific factor of the ubiquitin-mediated proteasomal degradation of activated RhoA. We further show that the cancer cell lines HEp-2, human embryonic kidney 293 and Vero are specifically deficient in ubiquitylation of either activated Rac, Cdc42, or Rho, respectively. In contrast, CNF1 produced the cellular depletion of all three isoforms of Rho proteins in the primary human cell types we have tested. We demonstrate that ectopic expression of Smurf1 in Vero cells, deficient for RhoA ubiquitylation, restores ubiquitylation of the activated forms of RhoA. We conclude here that Smurf1 ubiquitylates activated RhoA and that, in contrast to human primary cell types, some cancer cell lines have a lower ubiquitylation capacity of specific Rho proteins. Thus, both CNF1 and transforming growth factor-beta trigger activated RhoA ubiquitylation through Smurf1 ubiquitin-ligase.
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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.