ArticleBMC molecular biology2008
Differential regulation of the two transcriptional activation domains of the coiled-coil coactivator CoCoA by sumoylation.
Article in BMC molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Article
- CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel pathway for GATA1 function.Genes to cells : devoted to molecular & cellular mechanisms · 2014Article
- SUMOylation of ZFP282 potentiates its positive effect on estrogen signaling in breast tumorigenesis.Oncogene · 2013Article
- Modification of small hepatitis delta virus antigen by SUMO protein.Journal of virology · 2010Article
- SHIP2 (SH2 domain-containing inositol phosphatase 2) SH2 domain negatively controls SHIP2 monoubiquitination in response to epidermal growth factor.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe coiled-coil coactivator (CoCoA) enhances transcriptional activity of nuclear receptors, the xenobiotic aryl hydrocarbon receptor, and the lymphocyte enhancer factors (LEF) in the Wnt/beta-catenin signaling pathway. CoCoA is comprised of a large central coiled coil domain flanked by N-terminal and C-terminal activation domains (AD). The N-terminal AD of CoCoA is required for coactivator function with LEF and beta-catenin, while the C-terminal AD of CoCoA is required for coactivator function with nuclear receptors. We explored the role of sumoylation in regulating the activities of the two ADs and the coactivator function of CoCoA.
resultsThe N-terminus of CoCoA is covalently modified by SUMO1 at Lys-29; both PIAS1 and ARIP3 function as E3 ligases. Fusion of SUMO1 to the N-terminus (mimicking sumoylation) reduced coactivator function of CoCoA with LEF1 and the activity of the N-terminal AD. The N- and C-termini of CoCoA can bind to each other, and C-terminal transactivation activity is attenuated in the presence of the N-terminus, indicating that the N-C interaction regulates the activity of the C-terminal AD. Fusion of SUMO1 to the N-terminal fragment of CoCoA reduced the N-C interaction and inhibition of C-terminal AD activity by the N-terminal fragment.
conclusionSumoylation of CoCoA differentially regulates the coactivator activity of CoCoA with nuclear receptors versus LEF1, by attenuating the N-terminal AD activity and enhancing the activity of the C-terminal AD.
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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.