ArticleThe Journal of biological chemistry2010
A small ubiquitin-related modifier-interacting motif functions as the transcriptional activation domain of Krüppel-like factor 4.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- MBNL2 promotes aging-related cardiac fibrosis via inhibited SUMOylation of Krüppel-like factor4.iScience · 2024Article
- New insights into KLFs and SOXs in cancer pathogenesis, stemness, and therapy.Seminars in cancer biology · 2023Review
- Review
- KLF4 protein stability regulated by interaction with pluripotency transcription factors overrides transcriptional control.Genes & development · 2019Article
- KLF4 Regulates Corneal Epithelial Cell Cycle Progression by Suppressing Canonical TGF-β Signaling and Upregulating CDK Inhibitors P16 and P27.Investigative ophthalmology & visual science · 2019Article
- The post-translational modification, SUMOylation, and cancer (Review).International journal of oncology · 2018Review
- Klf4 glutamylation is required for cell reprogramming and early embryonic development in mice.Nature communications · 2018Article
- Review
- SUMOylation of KLF4 promotes IL-4 induced macrophage M2 polarization.Cell cycle (Georgetown, Tex.) · 2017Article
- Differentiation-Dependent KLF4 Expression Promotes Lytic Epstein-Barr Virus Infection in Epithelial Cells.PLoS pathogens · 2015Article
- miR-200c-SUMOylated KLF4 feedback loop acts as a switch in transcriptional programs that control VSMC proliferation.Journal of molecular and cellular cardiology · 2015Article
- Krüppel-like factor 4 regulates genetic stability in mouse embryonic fibroblasts.Molecular cancer · 2013Article
- Sumoylation of Krüppel-like factor 4 inhibits pluripotency induction but promotes adipocyte differentiation.The Journal of biological chemistry · 2013Article
- The roles of the reprogramming factors Oct4, Sox2 and Klf4 in resetting the somatic cell epigenome during induced pluripotent stem cell generation.Genome biology · 2012Review
- Small ubiquitin-like modifier (SUMO) modification of zinc finger protein 131 potentiates its negative effect on estrogen signaling.The Journal of biological chemistry · 2012Article
- Novel insight into KLF4 proteolytic regulation in estrogen receptor signaling and breast carcinogenesis.The Journal of biological chemistry · 2012Article
- SUMOylation represses Nanog expression via modulating transcription factors Oct4 and Sox2.PloS one · 2012Article
- The E3 ubiquitin ligase SMAD ubiquitination regulatory factor 2 negatively regulates Krüppel-like factor 5 protein.The Journal of biological chemistry · 2011Article
- Regulation of Krüppel-like factor 4 by the anaphase promoting complex pathway is involved in TGF-beta signaling.The Journal of biological chemistry · 2011Article
- Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
The zinc finger transcription factor, Krüppel-like factor 4 (KLF4), regulates numerous biological processes, including proliferation, differentiation, and embryonic stem cell self-renewal. Although the DNA sequence to which KLF4 binds is established, the mechanism by which KLF4 controls transcription is not well defined. Small ubiquitin-related modifier (SUMO) is an important regulator of transcription. Here we show that KLF4 is both SUMOylated at a single lysine residue and physically interacts with SUMO-1 in a region that matches an acidic and hydrophobic residue-rich SUMO-interacting motif (SIM) consensus. The SIM in KLF4 is required for transactivation of target promoters in a SUMO-1-dependent manner. Mutation of either the acidic or hydrophobic residues in the SIM significantly impairs the ability of KLF4 to interact with SUMO-1, activate transcription, and inhibit cell proliferation. Our study provides direct evidence that SIM in KLF4 functions as a transcriptional activation domain. A survey of transcription factor sequences reveals that established transactivation domains of many transcription factors contain sequences highly related to SIM. These results, therefore, illustrate a novel mechanism by which SUMO interaction modulates the activity of transcription factors.
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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.