New ligands of the cellular retinoic acid-binding protein 2 (CRABP2) suggest a role for this protein in chromatin remodeling

• Autor(a) principal: Rossetto, Daniella de Barros [UNESP]
• Data de Publicação: 2014
• Outros Autores: Kiyomoto, Eric Nishimura [UNESP], Carvalho, Carlos Eduardo Brantis de [UNESP], Zanelli, Cleslei Fernando [UNESP], Valentini, Sandro Roberto [UNESP]
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNESP
• Texto Completo: http://serv-bib.fcfar.unesp.br/seer/index.php/Cien_Farm/article/view/371; http://hdl.handle.net/11449/123635
• topic: CRABP2; Saccharomyces cerevisiae and twohybrid system

Retinoic acid (RA) regulates the transcription of a series of genes involved in cell proliferation, differentiation and apoptosis by binding to the RA Receptor (RAR) and Retinoid X Receptor (RXR) heterodimers. The cellular retinoic acid-binding protein 2 (CRABP2) is involved in the transport of RA from the cytosol to specific RA receptors in the nucleus, acting as a coactivator of nuclear retinoid receptors. In order to have a better understanding of the role of CRABP2 in RA signaling, we used the yeast two-hybrid system as a tool for the identification of physical protein-protein interactions. Twenty-three putative CRABP2-interacting proteins were identified by screening in the presence of RA, five of which are related to transcription regulation or, more specifically, to the process of chromatin remodeling: t-complex 1 (TCP1); H3 histone, family 3A (H3F3A); H3 histone, family 3B (H3F3B); β-tubulin (TUBB) and SR-related CTD-associated factor 1 (SCAF1). These results suggest a more direct role for CRABP2 in chromatin remodeling and may be a starting point for the elucidation of the fine-tuning control of transcription by RA receptors.