ArticleScientific reports2017
Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- How intrinsically disordered regions shape the function of CREB-binding protein.Biochemical Society transactions · 2026Review
- ATRX: From Chromatin Remodeling to Disease.Genesis (New York, N.Y. : 2000) · 2025Review
- Decoding Order and Disorder in Proteins by NMR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Review
- A cyclin D1 intrinsically disordered domain accesses modified histone motifs to govern gene transcription.Oncogenesis · 2024Article
- Chromatin Sensing by the Auxiliary Domains of KDM5C Regulates Its Demethylase Activity and Is Disrupted by X-linked Intellectual Disability Mutations.Journal of molecular biology · 2023Article
- Chemistry towards Biology-Instruct: Snapshot.International journal of molecular sciences · 2022Review
- NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering.Biomolecules · 2022Article
- Review
- Characterization of intrinsically disordered regions in proteins informed by human genetic diversity.PLoS computational biology · 2022Article
- Novel diagnostic DNA methylation episignatures expand and refine the epigenetic landscapes of Mendelian disorders.HGG advances · 2022Article
- FOXN1 forms higher-order nuclear condensates displaced by mutations causing immunodeficiency.Science advances · 2021Article
- Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues.Magnetic resonance (Gottingen, Germany) · 2021Article
- The long-standing relationship between paramagnetic NMR and iron-sulfur proteins: the mitoNEET example. An old method for new stories or the other way around?Magnetic resonance (Gottingen, Germany) · 2021Article
- Article
- A Switch between Two Intrinsically Disordered Conformational Ensembles Modulates the Active Site of a Basic-Helix-Loop-Helix Transcription Factor.The journal of physical chemistry letters · 2020Article
- Directional divergence of Ep300 duplicates in teleosts and its implications.BMC evolutionary biology · 2020Article
- Unraveling the molecular interactions involved in phase separation of glucocorticoid receptor.BMC biology · 2020Article
- Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.Journal of molecular biology · 2020Review
- Interaction between the scaffold proteins CBP by IQGAP1 provides an interface between gene expression and cytoskeletal activity.Scientific reports · 2020Article
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11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The multi-domain transcriptional coactivators CBP/p300 integrate a multitude of signaling inputs, interacting with more than 400 proteins via one or more of their globular domains. While CBP/p300 function is typically considered in terms of these structured domains, about half of the protein consists of intrinsically disordered regions (IDRs) of varying length. However, these IDRs have only been thought of as linkers that allow flexible spatial arrangement of the structured domains, but recent studies have shown that similar IDRs mediate specific and critical interactions in other proteins. To examine the roles of IDRs in CBP, we performed yeast-two-hybrid screenings of placenta and lung cancer cDNA libraries, which demonstrated that the long IDR linking the KIX domain and bromodomain of CBP (termed ID3) can potentially bind to several proteins. The RNA-binding Zinc-finger protein 106 (ZFP106) detected in both libraries was identified as a novel substrate for CBP-mediated acetylation. Nuclear magnetic resonance (NMR) spectroscopy combined with cross-linking experiments and competition-binding assays showed that the fully disordered isolated ID3 transiently interacts with an IDR of ZFP106 in a fashion that disorder of both regions is maintained. These findings demonstrate that beside the linking function, ID3 can also interact with acetylation substrates of CBP.
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