ArticleThe Biochemical journal2004
The CBP/p300 TAZ1 domain in its native state is not a binding partner of MDM2.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Cited2 is a key regulator of placental development and plasticity.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024Review
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- Pitfalls at Chemistry of Adenoviral Vector Vaccine against COVID-19 and How to Circumvent it.Advanced pharmaceutical bulletin · 2022Article
- Role of CITED2 in stem cells and cancer.Oncology letters · 2020Review
- Article
- Proteins interacting with cloning scars: a source of false positive protein-protein interactions.Scientific reports · 2015Article
- The high-risk HPV16 E7 oncoprotein mediates interaction between the transcriptional coactivator CBP and the retinoblastoma protein pRb.Journal of molecular biology · 2014Article
- Structural characterization of interactions between the double-stranded RNA-binding zinc finger protein JAZ and nucleic acids.Biochemistry · 2014Article
- Advancements in the development of HIF-1α-activated protein switches for use in enzyme prodrug therapy.PloS one · 2014Article
- Hybrid dynamics simulation engine for metalloproteins.Biophysical journal · 2012Article
- Mdm2 and MdmX as Regulators of Gene Expression.Genes & cancer · 2012Article
- Ubiquitous [Na+]i/[K+]i-sensitive transcriptome in mammalian cells: evidence for Ca(2+)i-independent excitation-transcription coupling.PloS one · 2012Article
- Disrupting the CH1 domain structure in the acetyltransferases CBP and p300 results in lean mice with increased metabolic control.Cell metabolism · 2011Article
- Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Two distinct motifs within the p53 transactivation domain bind to the Taz2 domain of p300 and are differentially affected by phosphorylation.Biochemistry · 2009Article
- A protein methylation pathway in Chlamydomonas flagella is active during flagellar resorption.Molecular biology of the cell · 2008Article
- The zinc finger proteins ZXDA and ZXDC form a complex that binds CIITA and regulates MHC II gene transcription.Journal of molecular biology · 2007Article
- Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Conditional knockout mice reveal distinct functions for the global transcriptional coactivators CBP and p300 in T-cell development.Molecular and cellular biology · 2006Article
- Two transactivation mechanisms cooperate for the bulk of HIF-1-responsive gene expression.The EMBO journal · 2005Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
The transcriptional co-activator CBP [CREB (cAMP-response-element-binding protein)-binding protein] and its paralogue p300 play a key role in the regulation of both activity and stability of the tumour suppressor p53. Degradation of p53 is mediated by the ubiquitin ligase MDM2 (mouse double minute protein) and is also reported to be regulated by CBP/p300. Direct protein-protein interaction between a central domain of MDM2 and the TAZ1 (transcriptional adaptor zinc-binding domain) [C/H1 (cysteine/histidine-rich region 1)] domain of p300 and subsequent formation of a ternary complex including p53 have been reported previously. We expressed and purified the proposed binding domains of HDM2 (human homologue of MDM2) and CBP, and examined their interactions using CD spectroscopy. The binding studies were extended by using natively purified GST (glutathione S-transferase)-p300 TAZ1 and GST-p53 fusion proteins, together with in vitro translated HDM2 fragments, under similar solution conditions to those in previous studies, but omitting added EDTA, which causes unfolding and aggregation of the zinc-binding TAZ1 domain. Comparing the binding properties of the known TAZ1 interaction partners HIF-1alpha (hypoxia-inducible factor 1), CITED2 (CBP/p300-interacting transactivator with glutamic- and aspartic-rich tail) and STAT2 (signal transducer and activator of transcription 2) with HDM2, our data suggest that TAZ1 in its native state does not serve as a specific recognition domain of HDM2. Rather, unfolded TAZ1 and HDM2 proteins have a high tendency to aggregate, and non-specific protein complexes are formed under certain conditions.
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