Unique protein interaction networks define the chromatin remodelling module of the NuRD complex

Unique protein interaction networks define the chromatin remodelling module of the NuRD complex.

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Item Type: Article
Status: Published
Official URL: https://doi.org/10.1111/febs.16112
Journal or Publication Title: The FEBS Journal
Date: 7 July 2021
Divisions: Gene and Stem Cell Therapy
Cancer and Gene Regulation
Depositing User: General Admin
Identification Number: 10.1111/febs.16112
ISSN: 1742-464X
Date Deposited: 10 Oct 2021 10:45

The combination of four proteins and their paralogues including MBD2/3, GATAD2A/B, CDK2AP1 and CHD3/4/5, which we refer to as the MGCC module, form the chromatin remodelling module of the nucleosome remodelling and deacetylase (NuRD) complex. To date, mechanisms by which the MGCC module acquires paralogue-specific function and specificity have not been addressed. Understanding the protein-protein interaction (PPI) network of the MGCC subunits is essential for defining underlying mechanisms of gene regulation. Therefore, using pulldown followed by mass spectrometry analysis (PD-MS), we report a proteome-wide interaction network of the MGCC module in a paralogue-specific manner. Our data also demonstrate that the disordered C-terminal region of CHD3/4/5 is a gateway to incorporate remodelling activity into both ChAHP (CHD4, ADNP, HP1γ) and NuRD complexes in a mutually exclusive manner. We define a short aggregation-prone region (APR) within the C-terminal segment of GATAD2B that is essential for the interaction of CHD4 and CDK2AP1 with the NuRD complex. Finally, we also report an association of CDK2AP1 with the nuclear receptor co-repressor (NCOR) complex. Overall, this study provides insight into the possible mechanisms through which the MGCC module can achieve specificity and diverse biological functions.

Keywords: CHD4; ChAHP complex; NCOR complex; NuRD complex; aggregation prone region; chromatin remodelling; protein-protein interactions.

© 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

Sharifi Tabar, Mehdi
Giardina, Caroline
Feng, Yue
Francis, Habib
Moghaddas Sani, Hakimeh
Low, Jason K. K.
Mackay, Joel P.
Bailey, Charles G.
Rasko, John E. J.
Last Modified: 12 Oct 2021 06:03
URI: https://eprints.centenary.org.au/id/eprint/1086

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