ArticleNucleic acids research2010
PIAS1 regulates CP2c localization and active promoter complex formation in erythroid cell-specific alpha-globin expression.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- A Cell-Penetrant Peptide Disrupting the Transcription Factor CP2c Complexes Induces Cancer-Specific Synthetic Lethality.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- SUMOylation-mediated PSME3-20Science advances · 2023Article
- Structural and Functional Insights into CP2c Transcription Factor Complexes.International journal of molecular sciences · 2022Article
- YY1 and CP2c in Unidirectional Spermatogenesis and Stemness.Development & reproduction · 2020Review
- Rational discovery of antimetastatic agents targeting the intrinsically disordered region of MBD2.Science advances · 2019Article
- Article
- Mbd2-CP2c loop drives adult-type globin gene expression and definitive erythropoiesis.Nucleic acids research · 2018Article
- Diagnostic and prognostic relevance of CP2c and YY1 expression in hepatocellular carcinoma.Oncotarget · 2017Article
- MicroRNA-144 is regulated by CP2 and decreases COX-2 expression and PGE2 production in mouse ovarian granulosa cells.Cell death & disease · 2017Article
- The transcription factor LSF: a novel oncogene for hepatocellular carcinoma.American journal of cancer research · 2012Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Data presented here extends our previous observations on α-globin transcriptional regulation by the CP2 and PIAS1 proteins. Using RNAi knockdown, we have now shown that CP2b, CP2c and PIAS1 are each necessary for synergistic activation of endogenous α-globin gene expression in differentiating MEL cells. In this system, truncated PIAS1 mutants lacking the ring finger domain recruited CP2c to the nucleus, as did wild-type PIAS1, demonstrating that this is a sumoylation-independent process. In vitro, recombinant CP2c, CP2b and PIAS1 bound DNA as a stable CBP (CP2c/CP2b/PIAS1) complex. Following PIAS1 knockdown in MEL cells, however, the association of endogenous CP2c and CP2b with the α-globin promoter simultaneously decreased. By mapping the CP2b- and CP2c-binding domains on PIAS1, and the PIAS1-binding domains on CP2b and CP2c, we found that two regions of PIAS1 that interact with CP2c/CP2b are required for its co-activator function. We propose that CP2c, CP2b, and PIAS1 form a hexametric complex with two units each of CP2c, CP2b, and PIAS1, in which PIAS1 serves as a clamp between two CP2 proteins, while CP2c binds directly to the target DNA and CP2b mediates strong transactivation.
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