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Subcellular sorting of the G-protein coupled mouse somatostatin receptor 5 by a network of PDZ-domain containing proteins

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Subcellular sorting of the G-protein coupled mouse somatostatin receptor 5 by a network of PDZ-domain containing proteins. / Bauch, Carola; Koliwer, Judith; Buck, Friedrich; Hönck, Hans-Hinrich; Kreienkamp, Hans-Jürgen.

In: PLOS ONE, Vol. 9, No. 2, 11.02.2014, p. e88529.

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

Harvard

Bauch, C, Koliwer, J, Buck, F, Hönck, H-H & Kreienkamp, H-J 2014, 'Subcellular sorting of the G-protein coupled mouse somatostatin receptor 5 by a network of PDZ-domain containing proteins', PLOS ONE, vol. 9, no. 2, pp. e88529. https://doi.org/10.1371/journal.pone.0088529

APA

Bauch, C., Koliwer, J., Buck, F., Hönck, H-H., & Kreienkamp, H-J. (2014). Subcellular sorting of the G-protein coupled mouse somatostatin receptor 5 by a network of PDZ-domain containing proteins. PLOS ONE, 9(2), e88529. https://doi.org/10.1371/journal.pone.0088529

Vancouver

Bauch C, Koliwer J, Buck F, Hönck H-H, Kreienkamp H-J. Subcellular sorting of the G-protein coupled mouse somatostatin receptor 5 by a network of PDZ-domain containing proteins. PLOS ONE. 2014 Feb 11;9(2):e88529. https://doi.org/10.1371/journal.pone.0088529

Bibtex

@article{91636d0cf0bb4355b754b9efc8ab2340,
title = "Subcellular sorting of the G-protein coupled mouse somatostatin receptor 5 by a network of PDZ-domain containing proteins",
abstract = "PSD-95/discs large/ZO-1 (PDZ) domain proteins integrate many G-protein coupled receptors (GPCRs) into membrane associated signalling complexes. Additional PDZ proteins are involved in intracellular receptor trafficking. We show that three PDZ proteins (SNX27, PIST and NHERF1/3) regulate the mouse somatostatin receptor subtype 5 (SSTR5). Whereas the PDZ ligand motif of SSTR5 is not necessary for plasma membrane targeting or internalization, it protects the SSTR5 from postendocytic degradation. Under conditions of lysosomal inhibition, recycling of the SSTR5 to the plasma membrane does not depend on the PDZ ligand. However, recycling of the wild type receptor carrying the PDZ binding motif depends on SNX27 which interacts and colocalizes with the receptor in endosomal compartments. PIST, implicated in lysosomal targeting of some membrane proteins, does not lead to degradation of the SSTR5. Instead, overexpressed PIST retains the SSTR5 at the Golgi. NHERF family members release SSTR5 from retention by PIST, allowing for plasma membrane insertion. Our data suggest that PDZ proteins act sequentially on the GPCR at different stages of its subcellular trafficking.",
author = "Carola Bauch and Judith Koliwer and Friedrich Buck and Hans-Hinrich H{\"o}nck and Hans-J{\"u}rgen Kreienkamp",
year = "2014",
month = feb,
day = "11",
doi = "10.1371/journal.pone.0088529",
language = "English",
volume = "9",
pages = "e88529",
journal = "PLOS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "2",

}

RIS

TY - JOUR

T1 - Subcellular sorting of the G-protein coupled mouse somatostatin receptor 5 by a network of PDZ-domain containing proteins

AU - Bauch, Carola

AU - Koliwer, Judith

AU - Buck, Friedrich

AU - Hönck, Hans-Hinrich

AU - Kreienkamp, Hans-Jürgen

PY - 2014/2/11

Y1 - 2014/2/11

N2 - PSD-95/discs large/ZO-1 (PDZ) domain proteins integrate many G-protein coupled receptors (GPCRs) into membrane associated signalling complexes. Additional PDZ proteins are involved in intracellular receptor trafficking. We show that three PDZ proteins (SNX27, PIST and NHERF1/3) regulate the mouse somatostatin receptor subtype 5 (SSTR5). Whereas the PDZ ligand motif of SSTR5 is not necessary for plasma membrane targeting or internalization, it protects the SSTR5 from postendocytic degradation. Under conditions of lysosomal inhibition, recycling of the SSTR5 to the plasma membrane does not depend on the PDZ ligand. However, recycling of the wild type receptor carrying the PDZ binding motif depends on SNX27 which interacts and colocalizes with the receptor in endosomal compartments. PIST, implicated in lysosomal targeting of some membrane proteins, does not lead to degradation of the SSTR5. Instead, overexpressed PIST retains the SSTR5 at the Golgi. NHERF family members release SSTR5 from retention by PIST, allowing for plasma membrane insertion. Our data suggest that PDZ proteins act sequentially on the GPCR at different stages of its subcellular trafficking.

AB - PSD-95/discs large/ZO-1 (PDZ) domain proteins integrate many G-protein coupled receptors (GPCRs) into membrane associated signalling complexes. Additional PDZ proteins are involved in intracellular receptor trafficking. We show that three PDZ proteins (SNX27, PIST and NHERF1/3) regulate the mouse somatostatin receptor subtype 5 (SSTR5). Whereas the PDZ ligand motif of SSTR5 is not necessary for plasma membrane targeting or internalization, it protects the SSTR5 from postendocytic degradation. Under conditions of lysosomal inhibition, recycling of the SSTR5 to the plasma membrane does not depend on the PDZ ligand. However, recycling of the wild type receptor carrying the PDZ binding motif depends on SNX27 which interacts and colocalizes with the receptor in endosomal compartments. PIST, implicated in lysosomal targeting of some membrane proteins, does not lead to degradation of the SSTR5. Instead, overexpressed PIST retains the SSTR5 at the Golgi. NHERF family members release SSTR5 from retention by PIST, allowing for plasma membrane insertion. Our data suggest that PDZ proteins act sequentially on the GPCR at different stages of its subcellular trafficking.

U2 - 10.1371/journal.pone.0088529

DO - 10.1371/journal.pone.0088529

M3 - SCORING: Journal article

C2 - 24523912

VL - 9

SP - e88529

JO - PLOS ONE

JF - PLOS ONE

SN - 1932-6203

IS - 2

ER -