Roger White

TL;DR: Reduction in the levels of RIP140 or prevention of its recruitment to nuclear receptors may provide novel mechanisms for the control of energy expenditure in adipose cells.

TL;DR: It is demonstrated that RIP140 interacts directly with PGC-1α and suppresses its activity, providing a mechanism for regulating target gene transcription via nuclear receptor-dependent and -independent pathways.

TL;DR: It is proposed that this tyrosine is required to maintain the receptor in a transcriptionally inactive state in the absence of hormone, and modification of this residue may generate a conformational change in the ligand‐binding domain of the receptor to form an interacting surface which allows the recruitment of co‐activators independent of hormone binding.

TL;DR: It is proposed that the pure antiestrogens inhibit receptor dimerization by means of their 7 alpha alkyl-amide extension, and it appears that as a consequence nuclear uptake is inhibited and the receptor more rapidly degraded in the cytoplasm.

TL;DR: RIP140-dependent control of proinflammatory gene expression via RelA/CBP may, therefore, represent a molecular rational for the cellular integration of metabolic and inflammatory pathways.