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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Master Transcription Regulators02:23

Master Transcription Regulators

Master transcription regulators are regulatory proteins that are predominantly responsible for regulating the expression of multiple genes. Often these genes work in concert to drive a  complex process. Activation of a master transcription regulator can lead to a cascade of transcriptional activation necessary for that outcome. These regulators can directly bind to the regulatory sequences of the various genes involved, or they can indirectly regulate transcription by binding to regulatory...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...

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Updated: Jun 13, 2026

Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer
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Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer

Published on: May 26, 2014

PAX3-FOXO1 Contacts BRD4 through Its Acetylated Intrinsically Disordered Region.

Olivia A Fraser1,2, Madeline N Schleicher1, Maya L Pagano1

  • 1Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, United States.

Biochemistry
|June 12, 2026
PubMed
Summary
This summary is machine-generated.

Post-translational modifications like acetylation in intrinsically disordered regions (IDRs) of transcription factors regulate protein function. This study identifies a new acetylation site on FOXO1, revealing its interaction with BRD4 and inhibition by JQ1.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Intrinsically disordered regions (IDRs) of transcription factors are key regulatory sites for post-translational modifications (PTMs).
  • Acetylation of the FOXO1 IDR in the PAX3-FOXO1 fusion protein stabilizes it and enhances transcriptional activity, driving alveolar rhabdomyosarcoma (ARMS).

Purpose of the Study:

  • To characterize acetylation in the FOXO1 IDR using nuclear magnetic resonance (NMR) spectroscopy.
  • To identify novel acetylation sites and investigate their interaction with BRD4.

Main Methods:

  • 13C direct-detect NMR spectroscopy was employed to analyze acetylation.
  • Protein-protein interactions between acetylated FOXO1 and BRD4 were studied.
  • The effect of the bromodomain and extraterminal domain inhibitor JQ1 was assessed.

Main Results:

  • A novel acetylation site at lysine 233 in endogenous FOXO1 was identified.
  • The first bromodomain of BRD4 was shown to bind to the acetylated region of FOXO1.
  • JQ1 was demonstrated to inhibit the interaction between BRD4 and acetylated FOXO1.

Conclusions:

  • Acetylation of FOXO1 at lysine 233 is a key regulatory event, potentially exposed in the PAX3-FOXO1 fusion protein.
  • The interaction between BRD4 and acetylated PAX3-FOXO1 at superenhancers in ARMS is mediated by BRD4's bromodomain.
  • These findings support the therapeutic potential of bromodomain and extraterminal domain inhibitors in cancer treatment.