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Molecular mechanisms of somatostatin receptor trafficking

Authors :
Pascal Dournaud
Zsolt Csaba
Stéphane Peineau
Source :
Journal of Molecular Endocrinology. 48:R1-R12
Publication Year :
2011
Publisher :
Bioscientifica, 2011.

Abstract

The neuropeptide somatostatin (SRIF) is an important modulator of neurotransmission in the central nervous system and acts as a potent inhibitor of hormone and exocrine secretion. In addition, SRIF regulates cell proliferation in normal and tumorous tissues. The six somatostatin receptor subtypes (sst1, sst2A, sst2B, sst3, sst4, and sst5), which belong to the G protein-coupled receptor (GPCR) family, share a common molecular topology: a hydrophobic core of seven transmembrane-spanning α-helices, three intracellular loops, three extracellular loops, an amino-terminus outside the cell, and a carboxyl-terminus inside the cell. For most of the GPCRs, intracytosolic sequences, and more particularly the C-terminus, are believed to interact with proteins that are mandatory for either exporting neosynthesized receptor, anchoring receptor at the plasma membrane, internalization, recycling, or degradation after ligand binding. Accordingly, most of the SRIF receptors can traffic not onlyin vitrowithin different cell types but alsoin vivo. A picture of the pathways and proteins involved in these processes is beginning to emerge.

Details

ISSN :
14796813 and 09525041
Volume :
48
Database :
OpenAIRE
Journal :
Journal of Molecular Endocrinology
Accession number :
edsair.doi.dedup.....7af996dad9791c81f79f7edc73c36f93