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Methyl-Cpg-Binding Domain As A Protein Interaction Partner In Promoter Regulation And Neurodevelopment Through Evolutionary Expanded Entanglement, Stephanie M. Bilinovich, Surya B. Chhetri, Jackson T. Mitchell, Gage O. Leighton, Vladislav Jdanov, Jacob K. Zieba, Taylor W. Cook, Krysta L. Engel, Robert M. Vaughan, Humza Bhatti, Sadie L. Heeringa, Amy M. Wilstermann, Sophie Vanderweele, Akansha S. Das, Emily C. Sherry, Stephen A. Duncan, Katie L. Uhl, David C. Hinds, Mark Mackiewicz, Sarah K. Meadows, Kimberly M. Newberry, E. Christopher Partridge, Sara G. Cline, C. Joy Shepard, D. Casey Smith, Antonio Bradley, Daniel Vogt, Daniel B. Campbell, Lucas Pozzo-Miller, Caleb P. Bupp, Austin J. Goodyke, Surender Rajasekaran, Rebecca C. Knickmeyer, Benjie Blair

Research, Publications & Creative Work

There is increasing evidence that the methyl-binding domain (MBD) is a protein-protein interaction motif that can function independently of methylated DNA binding. The MBD proteins found throughout plants and invertebrates duplicated into multiple vertebrate DNA and non-DNA-binding members (MBD1, MBD2, MBD3, MBD4, MBD5, MBD6, MECP2, BAZ2A, BAZ2B, SETDB1, andSETDB2). Although many invertebrate species possess MBD proteins that can bind and recognize DNA methylation, the DNA-binding function has been independently lost multiple times, with only minor alterations to the protein interaction residues. The nucleosome remodeling and deacetylase (NuRD) complex, which interacts with MBD2/3 and is colocalized with MBD1/4 ChIP-Seq, is maintained …