| http://purl.uniprot.org/citations/23557604 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23557604 | http://www.w3.org/2000/01/rdf-schema#comment | "β-Arrestins were identified as scaffold-proteins that have the capacity to desensitize G protein-coupled receptors. However, it has been found that β-arrestins activate signaling pathways independent of G protein activation. The diversity of these signaling pathways has also been recognized for receptor tyrosine kinase. The aim of the present study was to validate the β-arrestin-dependent signaling mechanism(s) responsible for regulation of adipogenesis. Two signal models were selected, ghrelin and insulin, based on its β-arrestin-associated Akt activity. Herein, we found that β-arrestin 1 and 2 were essential molecules for adipocyte differentiation. More specifically, the role of these scaffolding proteins was demonstrated by depletion of β-arrestin 1 and 2 during ghrelin-induced adipogenesis in 3T3-L1 cells, which decreased the adipocyte differentiation and the expression levels of master regulators of early, the CCAAT/enhancer-binding protein β (C/EBPβ) and the CCAAT/enhancer-binding protein δ (C/EBPδ), and terminal, the peroxisome proliferator-activated receptor (PPARγ) and the CCAAT/enhancer-binding protein α (C/EBPα), adipogenesis. Accordingly ghrelin-induced Akt activity and its downstream targets, the mammalian target of rapamycin complex 1 (mTORC1) and the ribosomal protein S6 kinase beta-1 (S6K1), were inhibited by β-arrestin 1 and 2 siRNAs. By contrast, assays performed during insulin-activated adipogenesis showed an intensifying effect on the adipocyte differentiation as well as on the expression of C/EBPβ, C/EBPδ, PPARγ and C/EBPα. The increase in insulin-induced adipogenesis by β-arrestin knock-down was concomitant to a decrease in the insulin receptor susbtrate-1 (IRS-1) serine phosphorylation, proving the loss of the negative feedback loop on IRS-1/phosphoinositide 3-kinase (PI3K)/Akt. Therefore, β-arrestins control the extent and intensity of the lipogenic and adipogenic factors associated to Akt signaling, although the mechanistic and functional principles that underlie the connection between signaling and β-arrestins are specifically associated to each receptor type."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.biocel.2013.03.014"xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/author | "Casanueva F.F."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/author | "Camina J.P."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/author | "Pazos Y."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/author | "Lodeiro M."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/author | "Gurriaran-Rodriguez U."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/author | "Mosteiro C.S."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/author | "Santos-Zas I."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/author | "Bouzo-Lorenzo M."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/author | "Casabiell X."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/name | "Int J Biochem Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/pages | "1281-1292"xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/title | "beta-Arrestin signal complex plays a critical role in adipose differentiation."xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://purl.uniprot.org/core/volume | "45"xsd:string |
| http://purl.uniprot.org/citations/23557604 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23557604 |
| http://purl.uniprot.org/citations/23557604 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23557604 |
| http://purl.uniprot.org/uniprot/#_A0A158SIT9-mappedCitation-23557604 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23557604 |
| http://purl.uniprot.org/uniprot/#_P35569-mappedCitation-23557604 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23557604 |
| http://purl.uniprot.org/uniprot/#_Q3U172-mappedCitation-23557604 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23557604 |
| http://purl.uniprot.org/uniprot/#_J3JS97-mappedCitation-23557604 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23557604 |
| http://purl.uniprot.org/uniprot/#_Q3TRC8-mappedCitation-23557604 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23557604 |
| http://purl.uniprot.org/uniprot/#_Q810H1-mappedCitation-23557604 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23557604 |