Interaction of the human somatostatin receptor 3 with the multiple PDZ domain protein MUPP1 enables somatostatin to control permeability of epithelial tight junctions.
The presence of heterotrimeric G-proteins at epithelial tight junctions suggests that these cellular junctions are regulated by so far unknown G-protein coupled receptors. We identify here an interaction between the human somatostatin receptor 3 (hSSTR3) and the multiple PDZ protein MUPP1. MUPP1 is a tight junction scaffold protein in epithelial ... cells, and as a result of the interaction with MUPP1 the hSSTR3 is targeted to tight junctions. Interaction with MUPP1 enables the receptor to regulate transepithelial permeability in a pertussis toxin sensitive manner, suggesting that hSSTR3 can activate G-proteins locally at tight junctions.
Mesh Terms:
Carrier Proteins, Epithelium, GTP-Binding Proteins, Humans, PDZ Domains, Permeability, Pertussis Toxin, Receptors, Somatostatin, Somatostatin, Tight Junctions, Two-Hybrid System Techniques
Carrier Proteins, Epithelium, GTP-Binding Proteins, Humans, PDZ Domains, Permeability, Pertussis Toxin, Receptors, Somatostatin, Somatostatin, Tight Junctions, Two-Hybrid System Techniques
FEBS Lett.
Date: Jan. 05, 2009
PubMed ID: 19071123
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