Interaction of the human somatostatin receptor 3 with the multiple PDZ domain protein MUPP1 enables somatostatin to control permeability of epithelial tight junctions

FEBS Lett. 2009 Jan 5;583(1):49-54. doi: 10.1016/j.febslet.2008.11.048. Epub 2008 Dec 9.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / metabolism*
  • Epithelium / drug effects
  • Epithelium / metabolism*
  • GTP-Binding Proteins / metabolism
  • Humans
  • Membrane Proteins
  • PDZ Domains
  • Permeability / drug effects
  • Pertussis Toxin / pharmacology
  • Receptors, Somatostatin / metabolism*
  • Somatostatin / metabolism*
  • Tight Junctions / metabolism*
  • Two-Hybrid System Techniques


  • Carrier Proteins
  • MPDZ protein, human
  • Membrane Proteins
  • Receptors, Somatostatin
  • somatostatin receptor 3
  • Somatostatin
  • Pertussis Toxin
  • GTP-Binding Proteins