Interaction of the human somatostatin receptor 3 with the multiple PDZ domain protein MUPP1 enables somatostatin to control permeability of epithelial tight junctions.
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Interaction of the human somatostatin receptor 3 with the multiple PDZ domain protein MUPP1 enables somatostatin to control permeability of epithelial tight junctions. / Vockel, Matthias; Liew, Chong Wee; Glassmeier, Günter; Brandner, Johanna; Fernandez-Ballester, Gregorio J; Schwarz, Jürgen R; Schulz, Stefan; Buck, Friedrich; Serrano, Luis; Richter, Dietmar; Kreienkamp, Hans-Jürgen.
in: FEBS LETT, Jahrgang 583, Nr. 1, 1, 2009, S. 49-54.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Interaction of the human somatostatin receptor 3 with the multiple PDZ domain protein MUPP1 enables somatostatin to control permeability of epithelial tight junctions.
AU - Vockel, Matthias
AU - Liew, Chong Wee
AU - Glassmeier, Günter
AU - Brandner, Johanna
AU - Fernandez-Ballester, Gregorio J
AU - Schwarz, Jürgen R
AU - Schulz, Stefan
AU - Buck, Friedrich
AU - Serrano, Luis
AU - Richter, Dietmar
AU - Kreienkamp, Hans-Jürgen
PY - 2009
Y1 - 2009
N2 - 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.
AB - 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.
M3 - SCORING: Zeitschriftenaufsatz
VL - 583
SP - 49
EP - 54
JO - FEBS LETT
JF - FEBS LETT
SN - 0014-5793
IS - 1
M1 - 1
ER -