Investigation of the interaction between CREB-binding protein and STAT4/STAT6

Related Experiment Video

Updated: Jun 6, 2026

Analysis of the c-KIT Ligand Promoter Using Chromatin Immunoprecipitation
09:40

Analysis of the c-KIT Ligand Promoter Using Chromatin Immunoprecipitation

Published on: June 27, 2017

Mingxiang Zhang1, Zhou Fu, Daiyin Tian

  • 1Department of Respiratory Medicine, Chongqing Medical University, Chongqing 400014, People's Republic of China.

Molecular Biology Reports
|December 9, 2010
PubMed

Insights

CREB-binding protein (CBP) directly interacts with STAT4, but not STAT6, via its C-terminal region. This interaction is crucial for STAT4 binding, offering insights into Th cytokine regulation.

Area of Science:

  • Molecular Biology
  • Immunology
  • Genetics

Background:

  • CREB-binding protein (CBP) is a transcriptional coactivator involved in regulating various transcription factors.
  • Signal transducer and activator of transcription factors (STATs) are crucial for immune responses, but their interaction mechanisms with CBP are not fully understood.

Purpose of the Study:

  • To investigate the direct interaction between CBP and STAT4/STAT6.
  • To identify the specific domains of CBP and STAT4 involved in their interaction.
  • To elucidate the role of STAT4's N-terminus in CBP binding.

Main Methods:

  • Yeast two-hybrid screening was employed to identify interacting proteins.
  • Specific CBP and STAT4/STAT6 fragments were constructed and tested for binding.
  • Immunoprecipitation assays were used to confirm direct interactions.

Main Results:

  • STAT4 directly interacts with the C-terminal fragment (residues 1678-2175) of CBP, which contains ZZ, TAZ2, and SID domains.
  • STAT6 does not interact with any tested CBP fragments.
  • The N-terminus of STAT4 is essential for its interaction with CBP.

Conclusions:

  • The study reveals a direct interaction between STAT4 and CBP, mediated by specific domains.
  • This interaction is dependent on the N-terminus of STAT4.
  • Findings contribute to understanding the molecular mechanisms underlying Th cytokine imbalance.

More Related Videos

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis10:22

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis

Published on: August 15, 2013

Investigation of Beige Fat Biology and Metabolism Using the CRISPR SunTag-p65-HSF1 Activation System09:52

Investigation of Beige Fat Biology and Metabolism Using the CRISPR SunTag-p65-HSF1 Activation System

Published on: January 6, 2023

Related Concept Videos

The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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...
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...
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...
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...