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Molecular mechanisms of somatostatin receptor trafficking
- 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.
- Subjects :
- Somatostatin receptor
Cell growth
Chemistry
media_common.quotation_subject
Intracellular Space
Cell biology
Protein Transport
Endocrinology
Somatostatin
Extracellular
Animals
Humans
Receptors, Somatostatin
Phosphorylation
Internalization
Receptor
Molecular Biology
Intracellular
Protein Binding
Signal Transduction
G protein-coupled receptor
media_common
Subjects
Details
- ISSN :
- 14796813 and 09525041
- Volume :
- 48
- Database :
- OpenAIRE
- Journal :
- Journal of Molecular Endocrinology
- Accession number :
- edsair.doi.dedup.....7af996dad9791c81f79f7edc73c36f93