Abstract
CTCF is a ubiquitous transcription factor that is involved in numerous, seemingly unrelated functions. These functions include, but are not limited to, positive or negative regulation of transcription, enhancer-blocking activities at developmentally regulated gene clusters and at imprinted loci, and X-chromosome inactivation. Here, we review recent data acquired with state-of-the-art technologies that illuminate possible mechanisms behind the diversity of CTCF functions. CTCF interacts with numerous protein partners, including cohesin, nucleophosmin, PARP1, Yy1 and RNA polymerase II. We propose that CTCF interacts with one or two different partners according to the biological context, applying the Roman principle of governance, 'divide and rule' (divide et impera).
Highlights
CCCTC-binding factor (CTCF) is a ubiquitously expressed 11-zincfinger vertebrate protein that binds to thousands of sites in the genome in a sequence-specific manner and performs myriad functions
We focus our attention on several protein partners of CTCF that are known to have important cellular functions, or that have been very recently identified [CTCF partners that have been identified in proteomic analysis only, such as lamin A/C, importins, topoisomerase II (Topo II) and others (Yusufzai et al, 2004), will not be covered]
poly[ADP-ribose] polymerase 1 (PARP1) stimulation might be of special interest, because PARP1 has been identified as a CTCF interaction partner (Yusufzai et al, 2004) and poly(ADP-ribosyl)ated forms of CTCF have been implicated in the control of transcription of imprinted genes and ribosomal DNA (Yu et al, 2004; Torrano et al, 2006; Caiafa and Zlatanova, 2009)
Summary
Summary CTCF is a ubiquitous transcription factor that is involved in numerous, seemingly unrelated functions. These functions include, but are not limited to, positive or negative regulation of transcription, enhancer-blocking activities at developmentally regulated gene clusters and at imprinted loci, and Xchromosome inactivation. We review recent data acquired with state-of-the-art technologies that illuminate possible mechanisms behind the diversity of CTCF functions. CTCF interacts with numerous protein partners, including cohesin, nucleophosmin, PARP1, Yy1 and RNA polymerase II. We propose that CTCF interacts with one or two different partners according to the biological context, applying the Roman principle of governance, ‘divide and rule’ (divide et impera)
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