ArticleNucleic acids research2006
Downstream signaling mechanism of the C-terminal activation domain of transcriptional coactivator CoCoA.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
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- C2H2-Type Zinc Finger Proteins: Evolutionarily Old and New Partners of the Nuclear Hormone Receptors.Nuclear receptor signaling · 2018Review
- 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
- Steroid receptor coactivators 1, 2, and 3: critical regulators of nuclear receptor activity and steroid receptor modulator (SRM)-based cancer therapy.Molecular and cellular endocrinology · 2012Review
- Transcriptional regulation of human dual specificity protein phosphatase 1 (DUSP1) gene by glucocorticoids.PloS one · 2010Article
- GAS, a new glutamate-rich protein, interacts differentially with SRCs and is involved in oestrogen receptor function.EMBO reports · 2009Article
- Modulation of Runx2 activity by estrogen receptor-alpha: implications for osteoporosis and breast cancer.Endocrinology · 2008Article
- CCAR1, a key regulator of mediator complex recruitment to nuclear receptor transcription complexes.Molecular cell · 2008Article
- Ligand-dependent interactions of the Ah receptor with coactivators in a mammalian two-hybrid assay.Toxicology and applied pharmacology · 2008Article
- Differential regulation of the two transcriptional activation domains of the coiled-coil coactivator CoCoA by sumoylation.BMC molecular biology · 2008Article
- Role of the N-terminal activation domain of the coiled-coil coactivator in mediating transcriptional activation by beta-catenin.Molecular endocrinology (Baltimore, Md.) · 2006Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The coiled-coil coactivator (CoCoA) is a transcriptional coactivator for nuclear receptors and enhances nuclear receptor function by the interaction with the bHLH-PAS domain (AD3) of p160 coactivators. The C-terminal activation domain (AD) of CoCoA possesses strong transactivation activity and is required for the coactivator function of CoCoA with nuclear receptors. To understand how CoCoA AD transmits its activating signal to the transcription machinery, we defined specific subregions, amino acid motifs and protein binding partners involved in the function of CoCoA AD. The minimal transcriptional AD was mapped to approximately 91 C-terminal amino acids and consists of acidic, serine/proline-rich and phenylalanine-rich subdomains. Transcriptional activation by the CoCoA AD was p300-dependent, and p300 interacted physically and functionally with CoCoA AD and was recruited to a promoter by the interaction with CoCoA AD. The FYDVASAF motif in the CoCoA AD was critical for the transcriptional activity of CoCoA AD, the interaction of CoCoA with p300, the coactivator function of CoCoA for estrogen receptor alpha and GRIP1 and the transcriptional synergy among coactivators GRIP1, CARM1, p300 and CoCoA. Taken together these data extend our understanding of the mechanism of downstream signaling by the essential C-terminal AD of the nuclear receptor coactivator CoCoA; they indicate that p300 is a functionally important interaction partner of CoCoA AD and that their interaction potentiates transcriptional activation by the p160 coactivator complex.
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