CBP/p300 in cell growth, transformation, and development.

By R. Goodman, S. Smolik. Genes & Development, 2000

1,845 citations recorded by the source corpus.

CREB binding protein (CBP) and p300 were both identified initially in protein interaction assays–the former through its association with the transcription factor CREB (Chrivia et al. 1993) and the latter through its interaction with the adenoviral-transforming protein E1A (Stein et al. 1990; Eckner et al. 1994). The recognition that these two proteins, one involved in transcription and the other in cell transformation, had highly conserved sequences suggested that they had the potential to participate in a variety of cellular functions (Fig. 1). Several excellent reviews (Janknecht and Hunter 1996; Shikama et al. 1997; Giles et al. 1998) have addressed the transcriptional coactivator functions of CBP/p300; this review focuses on the involvement of these proteins in the complex biological processes that affect cell growth, transformation, and development.

Subfields: Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/9a52d01f8abde19094ccfa4ec244640ab857464b

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Citations in the corpus

• Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies (2016, background): “The folded KIX domain of CBP is able to bind multiple transcription factors in vivo (58), most of which are intrinsically disordered.”
• NF-κB RelA Phosphorylation Regulates RelA Acetylation (2005, background): “In addition, RelA is phosphorylated in both the cytoplasm and the nucleus (23, 31, 34), whereas acetylation appears restricted to the nucleus, consistent with the nuclear localization of p300/CBP (14).”
• Modification of enhancer chromatin: what, how and why? (2013, background): “…(Ghisletti et al., 2010; Heintzman et al., 2009; Kim et al., 2010; Rada-Iglesias et al., 2011; Visel et al., 2009). p300/CBP are ubiquitously expressed and recruited, often cooperatively, by a broad range of sequence-dependent activators representing distinct TF classes (Goodman and Smolik, 2000).”
• Virtual Ligand Screening of the p300/CBP Histone Acetyltransferase: Identification of a Selective Small Molecule Inhibitor (2010, background): “…discovered as E1A onco- Chemistry & Biology 17, protein binding partners and cyclic AMP effectors, respectively (Goodman and Smolik, 2000). p300/CBP often serves as a transcriptional coactivator and has been suggested to bind to a range of important transcription factors (Goodman and Smolik, 2000).”
• HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention (2007, background): “…Lee and Workman, 2007). p300 (adenoviral E1A-associated protein of 300 kDa) and CBP (CREB-binding protein) form a pair of paralogous transcriptional coactivators and have been extensively reviewed elsewhere (Goodman and Smolik, 2000), so only the GNAT and MYST families are covered in this issue.”
• Lysine acetylation: codified crosstalk with other posttranslational modifications (2008, background): “Unlike the GNAT and MYST families, the p300/CBP group is unique to metazoans (Figure 2) (Goodman and Smolik, 2000).”