In:
Journal of Molecular Endocrinology, Bioscientifica, Vol. 48, No. 1 ( 2011-12-12), p. R1-R12
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 only in vitro within different cell types but also in vivo . A picture of the pathways and proteins involved in these processes is beginning to emerge.
Type of Medium:
Online Resource
ISSN:
0952-5041
,
1479-6813
Language:
Unknown
Publisher:
Bioscientifica
Publication Date:
2011
detail.hit.zdb_id:
1478171-2
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