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CBP-IDRs regulate acetylation and gene expression
Katie L Gelder1, Nicola A Carruthers1, Grace Gilbert2
1Molecular and Cellular Biology, School of Biosciences, The University of Sheffield, Sheffield S10 2TN, UK; Nucleic Acids Institute, The University of Sheffield, Sheffield S10 2TN, UK.
Cell Reports
|March 13, 2026
Summary
Intrinsically disordered regions (IDRs) in proteins like CBP cooperate to control nuclear functions. Their balance regulates gene expression, with disruption altering chromatin and acetylation patterns.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- Intrinsically disordered regions (IDRs) regulate protein function without stable structures.
- IDRs are crucial in multidomain proteins like CBP and EP300, but their cooperative mechanisms are unclear.
Purpose of the Study:
- To investigate how different IDRs within CBP cooperate to regulate complex nuclear behaviors.
- To understand the balance between positive and negative regulatory interactions within CBP condensates.
Main Methods:
- Analysis of CBP IDRs' sequence properties and their contribution to CBP behavior.
- Assessment of CBP condensate regulation and sensitivity to lysine acetylation.
- Evaluation of CBP's chromatin occupancy, histone acetylation, and gene expression.
Main Results:
- Distinct CBP IDRs with varying sequence properties contribute uniquely to CBP function.
- A critical balance between positive and negative regulatory interactions governs CBP condensates.
- Disrupting this balance alters CBP's chromatin binding, histone acetylation, and gene expression.
Conclusions:
- Different CBP IDRs exhibit intramolecular cooperation to control nuclear functions.
- The properties of IDRs critically shape the functional landscape of multidomain proteins like CBP.
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