J Mol Biol
School of Molecular and Microbial Biosciences, University of Sydney, Sydney, New South Wales 2006, Australia.
Published: January 2008
The C-terminal binding proteins (CtBPs) play roles in diverse cellular processes including transcriptional regulation, Golgi membrane fission, and synaptic ribbon formation. In the context of transcriptional regulation, they function as corepressors, interacting with promoter-bound transcription factors and recruiting a large protein complex that contains chromatin-modifying enzymes. We recently described the structure of a Thanatos-associated protein (THAP) domain that is found in a new member of the CtBP family, the Caenorhabditis elegans CTBP-1 protein. We have identified additional THAP domain-containing CtBPs in the nematode, echinoderm, and cephalochordate lineages. The distribution of these lineages within the animal kingdom suggests that the ancestral form of the animal CtBPs may have contained a THAP domain that was subsequently lost in the vertebrate and arthropod lineages. We also provide functional data indicating that CTBP-1 represses gene expression and homodimerizes and interacts with PXDLS-containing partner proteins, three key features of the previously characterized animal CtBPs. CTBP-1 is therefore the founding member of a new subgroup within the CtBP corepressor family, the THAP domain-containing CtBPs.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/j.jmb.2007.10.041 | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!
© LitMetric 2025. All rights reserved.