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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.

Standard

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, Vol. 583, No. 1, 1, 2009, p. 49-54.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Vockel, M, Liew, CW, Glassmeier, G, Brandner, J, Fernandez-Ballester, GJ, Schwarz, JR, Schulz, S, Buck, F, Serrano, L, Richter, D & Kreienkamp, H-J 2009, '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, vol. 583, no. 1, 1, pp. 49-54. <http://www.ncbi.nlm.nih.gov/pubmed/19071123?dopt=Citation>

APA

Vockel, M., Liew, C. W., Glassmeier, G., Brandner, J., Fernandez-Ballester, G. J., Schwarz, J. R., Schulz, S., Buck, F., Serrano, L., Richter, D., & Kreienkamp, H-J. (2009). 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, 583(1), 49-54. [1]. http://www.ncbi.nlm.nih.gov/pubmed/19071123?dopt=Citation

Vancouver

Vockel M, Liew CW, Glassmeier G, Brandner J, Fernandez-Ballester GJ, Schwarz JR et al. 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;583(1):49-54. 1.

Bibtex

@article{57bcc6d9b6c549ed86378ccde9056165,
title = "Interaction of the human somatostatin receptor 3 with the multiple PDZ domain protein MUPP1 enables somatostatin to control permeability of epithelial tight junctions.",
abstract = "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.",
author = "Matthias Vockel and Liew, {Chong Wee} and G{\"u}nter Glassmeier and Johanna Brandner and Fernandez-Ballester, {Gregorio J} and Schwarz, {J{\"u}rgen R} and Stefan Schulz and Friedrich Buck and Luis Serrano and Dietmar Richter and Hans-J{\"u}rgen Kreienkamp",
year = "2009",
language = "Deutsch",
volume = "583",
pages = "49--54",
journal = "FEBS LETT",
issn = "0014-5793",
publisher = "Elsevier",
number = "1",

}

RIS

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 -