Journal
FEBS LETTERS
Volume 583, Issue 1, Pages 49-54Publisher
WILEY
DOI: 10.1016/j.febslet.2008.11.048
Keywords
Heterotrimeric G-protein; PDZ domain; Tight junction
Funding
- DFG [Ri 192/24-1
- SFB545/B7]
- EC [QLG3-CT-1999-00908]
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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.
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