1. Nuclear Receptor Coregulators: Judges, Juries, and Executioners of Cellular Regulation 
David M. Lonard, Bert W. O'Malley 
Molecular Cell 
Volume 27, Issue 5, Pages (September 2007)
DOI: /j.molcel
Copyright © 2007 Elsevier Inc. Terms and Conditions

2. Figure 1 SRC-3, a PTM-Encoded Signal Integrator
Protein kinases (PKs) are activated by ligand-activated nuclear receptors (in a kinase cascade including IκB kinase [IKK]), growth factors, or other environmental signals, leading to SRC-3 phosphorylation (P) at distinct amino acid residues (red, green, and blue). These phosphorylations recruit other coactivator-associated proteins such as CBP/p300, CARM1, and ubiquitin ligases, resulting in the addition or loss of specific posttranslational modifications (PTMs) of SRC-3, including SUMOylation (Su), ubiquitination (Ub), methylation (Me), and acetylation (Ac) of SRC-3 and other members of the complex (Wu et al., 2004, 2006; Feng et al., 2006; Naeem et al., 2007). These specific phosphorylations comprise a PTM “code” that leads to the recruitment of distinct co-coactivators (CoX, CoY, or CoZ) (Wu et al., 2004). In conjunction with phosphorylation and Ub modification of SRC-3 and its co-coactivator cohorts (Wu et al., 2007), SRC-3 is postulated to lead to the coactivator complex's ability to selectively engage with distinct transcription factors such as nuclear receptors (NRs), nuclear factor-κB (NF-κB), or other transcription factors (TFs). Ultimately, these PTMs lead to complex disintegration by either dissociation or degradation (via the proteasome) of the coactivator complex. Coactivator complexes (or individual complex components) that are not degraded may be recycled.
Molecular Cell  , DOI: ( /j.molcel )
Copyright © 2007 Elsevier Inc. Terms and Conditions