Molecular mechanisms of somatostatin receptor trafficking

Journal of Molecular Endocrinology - Tập 48 Số 1 - Trang R1-R12 - 2012
Zsolt Csaba1,2, Stéphane Peineau3,1,2, Pascal Dournaud1,2
1INSERM, Unite ´Mixte de Recherche U676, Paris, France
2Universite ´de Me ´decine Denis Diderot-Paris 7, Paris, France
3Department of Anatomy, MRC Centre for Synaptic Plasticity, Bristol, UK

Tóm tắt

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.

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Thông tin xuất bản

Journal of Molecular Endocrinology

Tập 48 Số 1

R1-R12

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