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PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95: quantitative characterization of interactions

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PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95 : quantitative characterization of interactions. / Møller, Thor C; Wirth, Volker F; Roberts, Nina Ingerslev; Bender, Julia; Bach, Anders; Jacky, Birgitte P S; Strømgaard, Kristian; Deussing, Jan M; Schwartz, Thue W; Martinez, Karen L.

In: PLOS ONE, Vol. 8, No. 5, e63352, 2013.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Møller, TC, Wirth, VF, Roberts, NI, Bender, J, Bach, A, Jacky, BPS, Strømgaard, K, Deussing, JM, Schwartz, TW & Martinez, KL 2013, 'PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95: quantitative characterization of interactions' PLOS ONE, vol. 8, no. 5, e63352. https://doi.org/10.1371/journal.pone.0063352

APA

Møller, T. C., Wirth, V. F., Roberts, N. I., Bender, J., Bach, A., Jacky, B. P. S., ... Martinez, K. L. (2013). PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95: quantitative characterization of interactions. PLOS ONE, 8(5), [e63352]. https://doi.org/10.1371/journal.pone.0063352

Vancouver

Møller TC, Wirth VF, Roberts NI, Bender J, Bach A, Jacky BPS et al. PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95: quantitative characterization of interactions. PLOS ONE. 2013;8(5). e63352. https://doi.org/10.1371/journal.pone.0063352

Author

Møller, Thor C ; Wirth, Volker F ; Roberts, Nina Ingerslev ; Bender, Julia ; Bach, Anders ; Jacky, Birgitte P S ; Strømgaard, Kristian ; Deussing, Jan M ; Schwartz, Thue W ; Martinez, Karen L. / PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95 : quantitative characterization of interactions. In: PLOS ONE. 2013 ; Vol. 8, No. 5.

Bibtex

@article{307c84840d27484fa6fad7e599ee674e,
title = "PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95: quantitative characterization of interactions",
abstract = "G protein-coupled receptors (GPCRs) constitute the largest family of membrane proteins in the human genome. Their signaling is regulated by scaffold proteins containing PDZ domains, but although these interactions are important for GPCR function, they are still poorly understood. We here present a quantitative characterization of the kinetics and affinity of interactions between GPCRs and one of the best characterized PDZ scaffold proteins, postsynaptic density protein 95 (PSD-95), using fluorescence polarization (FP) and surface plasmon resonance (SPR). By comparing these in vitro findings with colocalization of the full-length proteins in cells and with previous studies, we suggest that the range of relevant interactions might extend to interactions with K i = 450 µM in the in vitro assays. Within this range, we identify novel PSD-95 interactions with the chemokine receptor CXCR2, the neuropeptide Y receptor Y2, and four of the somatostatin receptors (SSTRs). The interaction with SSTR1 was further investigated in mouse hippocampal neurons, where we found a clear colocalization between the endogenously expressed proteins, indicating a potential for further investigation of the role of this interaction. The approach can easily be transferred to other receptors and scaffold proteins and this could help accelerate the discovery and quantitative characterization of GPCR-PDZ interactions.",
author = "M{\o}ller, {Thor C} and Wirth, {Volker F} and Roberts, {Nina Ingerslev} and Julia Bender and Anders Bach and Jacky, {Birgitte P S} and Kristian Str{\o}mgaard and Deussing, {Jan M} and Schwartz, {Thue W} and Martinez, {Karen L}",
year = "2013",
doi = "10.1371/journal.pone.0063352",
language = "English",
volume = "8",
journal = "P L o S One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "5",

}

RIS

TY - JOUR

T1 - PDZ domain-mediated interactions of G protein-coupled receptors with postsynaptic density protein 95

T2 - quantitative characterization of interactions

AU - Møller, Thor C

AU - Wirth, Volker F

AU - Roberts, Nina Ingerslev

AU - Bender, Julia

AU - Bach, Anders

AU - Jacky, Birgitte P S

AU - Strømgaard, Kristian

AU - Deussing, Jan M

AU - Schwartz, Thue W

AU - Martinez, Karen L

PY - 2013

Y1 - 2013

N2 - G protein-coupled receptors (GPCRs) constitute the largest family of membrane proteins in the human genome. Their signaling is regulated by scaffold proteins containing PDZ domains, but although these interactions are important for GPCR function, they are still poorly understood. We here present a quantitative characterization of the kinetics and affinity of interactions between GPCRs and one of the best characterized PDZ scaffold proteins, postsynaptic density protein 95 (PSD-95), using fluorescence polarization (FP) and surface plasmon resonance (SPR). By comparing these in vitro findings with colocalization of the full-length proteins in cells and with previous studies, we suggest that the range of relevant interactions might extend to interactions with K i = 450 µM in the in vitro assays. Within this range, we identify novel PSD-95 interactions with the chemokine receptor CXCR2, the neuropeptide Y receptor Y2, and four of the somatostatin receptors (SSTRs). The interaction with SSTR1 was further investigated in mouse hippocampal neurons, where we found a clear colocalization between the endogenously expressed proteins, indicating a potential for further investigation of the role of this interaction. The approach can easily be transferred to other receptors and scaffold proteins and this could help accelerate the discovery and quantitative characterization of GPCR-PDZ interactions.

AB - G protein-coupled receptors (GPCRs) constitute the largest family of membrane proteins in the human genome. Their signaling is regulated by scaffold proteins containing PDZ domains, but although these interactions are important for GPCR function, they are still poorly understood. We here present a quantitative characterization of the kinetics and affinity of interactions between GPCRs and one of the best characterized PDZ scaffold proteins, postsynaptic density protein 95 (PSD-95), using fluorescence polarization (FP) and surface plasmon resonance (SPR). By comparing these in vitro findings with colocalization of the full-length proteins in cells and with previous studies, we suggest that the range of relevant interactions might extend to interactions with K i = 450 µM in the in vitro assays. Within this range, we identify novel PSD-95 interactions with the chemokine receptor CXCR2, the neuropeptide Y receptor Y2, and four of the somatostatin receptors (SSTRs). The interaction with SSTR1 was further investigated in mouse hippocampal neurons, where we found a clear colocalization between the endogenously expressed proteins, indicating a potential for further investigation of the role of this interaction. The approach can easily be transferred to other receptors and scaffold proteins and this could help accelerate the discovery and quantitative characterization of GPCR-PDZ interactions.

U2 - 10.1371/journal.pone.0063352

DO - 10.1371/journal.pone.0063352

M3 - Journal article

VL - 8

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 5

M1 - e63352

ER -

ID: 49468375