Regulation of GIP and GLP1 receptor cell surface expression by N-glycosylation and receptor heteromerization

In response to a meal, Glucose-dependent Insulinotropic Polypeptide (GIP) and Glucagon-like Peptide-1 (GLP-1) are released from gut endocrine cells into the circulation and interact with their cognate G-protein coupled receptors (GPCRs). Receptor activation results in tissue-selective pleiotropic re...

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Veröffentlicht in:	PloS one 2012-03, Vol.7 (3), p.e32675-e32675
Hauptverfasser:	Whitaker, Gina M, Lynn, Francis C, McIntosh, Christopher H S, Accili, Eric A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Augmentation Beta cells Binding sites Biology Bioluminescence Cell Line Cell surface Cercopithecus aethiops Consensus Sequence Cyclic AMP - biosynthesis Diabetes Endoplasmic reticulum Endoplasmic Reticulum - metabolism Energy consumption Energy transfer Epidermal growth factor Gene Expression Regulation GIP protein Glucagon Glucagon-like peptide 1 Glucagon-Like Peptide-1 Receptor Glucose Glycosylation Hostages Humans Insulin Insulin - metabolism Insulin Secretion Life sciences Ligands Medicine Membrane Glycoproteins - chemistry Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Molecular Sequence Data Mutagenesis Mutation N-Terminus Oligomerization Oligomers Pancreas Pancreatic beta cells Physiology Plasmids Polypeptides Potentiation Protein Isoforms Protein Multimerization Quality control Radioactive half-life Receptor mechanisms Receptors Receptors, Gastrointestinal Hormone - chemistry Receptors, Gastrointestinal Hormone - genetics Receptors, Gastrointestinal Hormone - metabolism Receptors, Glucagon - chemistry Receptors, Glucagon - genetics Receptors, Glucagon - metabolism Rodents Secretion Sequence Alignment Signal transduction
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