ArticleMolecular and cellular biology1998
Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 211 citations in OpenAlex.
- Total Chemical Synthesis of RNF4 by Sequential Native Chemical Ligation: C-To-N Versus N-To-C Strategies.The Journal of organic chemistry · 2026Article
- Paralogue-Specific Roles of SUMO1 and SUMO2/3 in Protein Quality Control and Associated Diseases.Cells · 2023Review
- Review
- The p97/VCP segregase is essential for arsenic-induced degradation of PML and PML-RARA.The Journal of cell biology · 2023Article
- PPT1 regulation of HSP90α depalmitoylation participates in the pathogenesis of hyperandrogenism.iScience · 2023Article
- A Plasmodium falciparum RING Finger E3 Ubiquitin Ligase Modifies the Roles of PfMDR1 and PfCRT in Parasite Drug Responses.Antimicrobial agents and chemotherapy · 2023Article
- JAG1 Intracellular Domain Enhances AR Expression and Signaling and Promotes Stem-like Properties in Prostate Cancer Cells.Cancers · 2022Article
- RNF4~RGMb~BMP6 axis required for osteogenic differentiation and cancer cell survival.Cell death & disease · 2022Article
- Identification of G protein-coupled receptor 55 (GPR55) as a target of curcumin.NPJ science of food · 2022Article
- Review
- The E3 Ubiquitin-Protein Ligase RNF4 Promotes TNF-α-Induced Cell Death Triggered by RIPK1.International journal of molecular sciences · 2021Article
- SUMO-Targeted Ubiquitin Ligases and Their Functions in Maintaining Genome Stability.International journal of molecular sciences · 2021Review
- Roles of Key Epigenetic Regulators in the Gene Transcription and Progression of Prostate Cancer.Frontiers in molecular biosciences · 2021Review
- RNF4 Regulates the BLM Helicase in Recovery From Replication Fork Collapse.Frontiers in genetics · 2021Article
- Dysregulation of Transcription Factor Activity During Formation of Cancer-Associated Fibroblasts.International journal of molecular sciences · 2020Article
- Resistance to second generation antiandrogens in prostate cancer: pathways and mechanisms.Cancer drug resistance (Alhambra, Calif.) · 2020Review
- Targeting the turnover of oncoproteins as a new avenue for therapeutics development in castration-resistant prostate cancer.Cancer letters · 2018Review
- Article
- SUMO-triggered ubiquitination of NR4A1 controls macrophage cell death.Cell death and differentiation · 2017Article
- Role of E2-RING Interactions in Governing RNF4-Mediated Substrate Ubiquitination.Journal of molecular biology · 2016Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using the DNA-binding domain of androgen receptor (AR) as a bait in a yeast two-hybrid screening, we have identified a small nuclear RING finger protein, termed SNURF, that interacts with AR in a hormone-dependent fashion in both yeast and mammalian cells. Physical interaction between AR and SNURF was demonstrated by coimmunoprecipitation from cell extracts and by protein-protein affinity chromatography. Rat SNURF is a highly hydrophilic protein consisting of 194 amino acid residues and comprising a consensus C3HC4 zinc finger (RING) structure in the C-terminal region and a bipartite nuclear localization signal near the N terminus. Immunohistochemical experiments indicated that SNURF is a nuclear protein. SNURF mRNA is expressed in a variety of human and rat tissues. Overexpression of SNURF in cultured mammalian cells enhanced not only androgen, glucocorticoid, and progesterone receptor-dependent transactivation but also basal transcription from steroid-regulated promoters. Mutation of two of the potential Zn2+ coordinating cysteines to serines in the RING finger completely abolished the ability of SNURF to enhance basal transcription, whereas its ability to activate steroid receptor-dependent transcription was maintained, suggesting that there are separate domains in SNURF that mediate interactions with different regulatory factors. SNURF is capable of interacting in vitro with the TATA-binding protein, and the RING finger domain is needed for this interaction. Collectively, we have identified and characterized a ubiquitously expressed RING finger protein, SNURF, that may function as a bridging factor and regulate steroid receptor-dependent transcription by a mechanism different from those of previously identified coactivator or integrator proteins.
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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.