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Proteomic analysis of phosphorylated nuclear proteins underscores novel roles for rapid actions of retinoic acid in the regulation of mRNA splicing and translation

AuthorsLaserna Mendieta, Emilio J.; Valero, María Luz; Sanz, Libia ; Sánchez del Pino, Manuel M.; Calvete, Juan J. ; Barettino, Domingo
KeywordsRetinoic Acid
nuclear hormone receptors
nongenomic actions
transcription-independent actions
alternative splicing
Issue Date7-Oct-2009
PublisherEndocrine Society
CitationMolecular Endocrinology 23(11):1799-814 (2009)
AbstractRetinoic acid (RA) signaling is mediated by the retinoic acid receptor (RAR),belonging to the nuclear hormone receptor superfamily. In addition to its classical transcriptional actions, RAR also mediates rapid tanscription-independent (nongenomic) actions, consisting in the activation of signal transduction pathways, as the phosphatidyl-inositol-3-kinase or the ERK MAPK-signaling pathways. RA-induced rapid transcription-independent actions play a role in different physiological contexts. As an effort toward understanding the functions of those rapid actions on signaling elicited by RA, we have identified nuclear proteins the phosphorylation state of which is rapidly modified by RA treatment in neuroblastoma cells, using a proteomic approach. Our results show that RA treatment led to changes in the phosphorylation patterns in two families of proteins: 1) those related to chromatin dynamics in relation to transcriptional activation, and 2) those related to mRNA processing and, in particular, mRNA splicing. We show that treatment of neuroblastoma cells with RA leads to alteration of the regulation of pre-mRNA splicing and mRNA translation. Thus, our results underscore novel functions for the rapid signaling elicited by RAR in the regulation of mRNA processing. We conclude that RA activation of signaling pathways can indeed regulate mRNA processing as part of a cellular response orchestrated by the nuclear receptor RAR
Description16 pages, 8 figures, 6 tables.- PMID: 19812389 [PubMed]
Publisher version (URL)http://dx.doi.org/10.1210/me.2009-0165
Appears in Collections:(IBV) Artículos
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