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Related Experiment Video

Updated: May 10, 2026

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Dido3 PHD modulates cell differentiation and division.

Jovylyn Gatchalian¹, Agnes Fütterer, Scott B Rothbart

¹Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.

|July 9, 2013

Summary

This summary is machine-generated.

Death Inducer Obliterator 3 (Dido3) regulates stemness genes in embryonic stem cells via its PHD finger binding to H3K4me3. Phosphorylation disrupts this binding, impacting cell division and genomic stability.

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Last Updated: May 10, 2026

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry

Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry

Published on: May 17, 2016

Area of Science:

Molecular Biology
Epigenetics
Cell Biology

Background:

Death Inducer Obliterator 3 (Dido3) plays a role in maintaining genomic stability and tumorigenesis.
Stem cell gene expression is crucial for development and disease.

Purpose of the Study:

To elucidate the mechanism by which Dido3 regulates stemness genes in embryonic stem cells.
To investigate the role of Dido3's plant homeodomain (PHD) finger in histone binding and its regulation.

Main Methods:

X-ray crystallography to determine the structure of Dido3 PHD bound to H3K4me3.
Biochemical assays to analyze binding affinity and specificity.
Mutational analysis to identify key residues in the binding mechanism.

Main Results:

Dido3's PHD finger binds to histone H3K4me3 through an atypical binding site.
Threonine phosphorylation disrupts Dido3-H3K4me3 binding, causing Dido3 to move from chromatin to the mitotic spindle.
Structural and biochemical data explain Dido3's specific binding and the inability of PHF3 to bind H3K4me3.

Conclusions:

Dido3's PHD finger interaction with H3K4me3 is a key regulator of stemness gene expression.
Post-translational modification (phosphorylation) of Dido3 links transcriptional control in development to cell division regulation.