G-protein-coupled receptors, cholesterol and palmitoylation: facts about fats. (Articolo in rivista)

Type
Label
  • G-protein-coupled receptors, cholesterol and palmitoylation: facts about fats. (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1677/JME-08-0114 (literal)
Alternative label
  • Chini B; Parenti M. (2009)
    G-protein-coupled receptors, cholesterol and palmitoylation: facts about fats.
    in Journal of molecular endocrinology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Chini B; Parenti M. (literal)
Pagina inizio
  • 371 (literal)
Pagina fine
  • 379 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 42 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CNR Inst Neurosci, Cellular & Mol Pharmacol Sect, I-20129 Milan, Italy Univ Milano Bicocca, Dept Expt Med, Monza, Italy (literal)
Titolo
  • G-protein-coupled receptors, cholesterol and palmitoylation: facts about fats. (literal)
Abstract
  • G-protein-coupled receptors (GPCRs) are integral membrane proteins, hence it is not surprising that a number of their structural and functional features are modulated by both proteins and lipids. The impact of interacting proteins and lipids on the assembly and signalling of GPCRs has been extensively investigated over the last 20-30 years, and a further impetus has been given by the proposal that GPCRs and/or their immediate signalling partners (G proteins) can partition within plasma membrane domains, termed rafts and caveolae, enriched in glycosphingolipids and cholesterol. The high content of these specific lipids, in particular of cholesterol, in the vicinity of GPCR transmembranes can affect GPCR structure and/or function. In addition, most GPCRs are post-translationally modified with one or more palmitic acid(s), a 16-carbon saturated fatty acid, covalently bound to cysteine(s) localised in the carboxyl-terminal cytoplasmic tail. The insertion of palmitate into the cytoplasmic leaflet of the plasma membrane can create a fourth loop, thus profoundly affecting GPCR structure and hence the interactions with intracellular partner proteins. This review briefly highlights how lipids of the membrane and the receptor themselves can influence GPCR organisation and functioning. (literal)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Autore CNR di
Prodotto
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Insieme di parole chiave di
data.CNR.it