Di/oligomerization of GPCRs-mechanisms and functional significance

Adolfo Rivero-Müller; Kim Carol Jonas; Aylin Carla Hanyaloglu; Ilpo Huhtaniemi

doi:10.1016/B978-0-12-386931-9.00007-6

Di/oligomerization of GPCRs-mechanisms and functional significance

Adolfo Rivero-Müller, Kim Carol Jonas, Aylin Carla Hanyaloglu, Ilpo Huhtaniemi

Women & Children's Health

From the Institute of Reproductive and Developmental Biology, Department of Surgery and Cancer, Imperial College London, Du Cane Road, London W12 0NN, United Kingdom, the Institute for Biomedicine, Department of Physiology, University of Turku, 20520 Turku, Finland [email protected].

Research output: Contribution to journal › Review article › peer-review

34 Citations (Scopus)

Abstract

Initially considered as strict and rigid monomers, GPCRs have shown an ever-increasing flexibility in the number of intermolecular interactions they can participate in. Few rules can be applied to all members of this receptor superfamily, as the functional roles of resulting dimers or oligomers vary widely from biosynthesis, functional complementation, enhancement and control of signaling, positive and negative cooperativity, signal desensitization, membrane trafficking, and pharmacological diversity, among others. Receptor dimerization/oligomerization is a challenging phenomenon to disentangle even in vitro and thus in vivo evidence for its functional significance requires employment of a variety of cutting-edge techniques. Nevertheless, the evidence for GPCR di/oligomerization at the physiological level is mounting and has begun to shed light on an intricate network of interactions that challenge the previous knowledge on how this family of receptors function. Here, we summarize the evidence for GPCR di/oligomerization in living organisms with a particular focus of their involvement in health and disease.

Original language	English
Pages (from-to)	163-85
Number of pages	23
Journal	Progress in molecular biology and translational science
Volume	117
DOIs	https://doi.org/10.1016/B978-0-12-386931-9.00007-6
Publication status	Published - 2013

Keywords

Animals
Cells/metabolism
Disease
Health
Humans
Models, Molecular
Protein Multimerization
Receptors, G-Protein-Coupled/chemistry

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10.1016/B978-0-12-386931-9.00007-6

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title = "Di/oligomerization of GPCRs-mechanisms and functional significance",

abstract = "Initially considered as strict and rigid monomers, GPCRs have shown an ever-increasing flexibility in the number of intermolecular interactions they can participate in. Few rules can be applied to all members of this receptor superfamily, as the functional roles of resulting dimers or oligomers vary widely from biosynthesis, functional complementation, enhancement and control of signaling, positive and negative cooperativity, signal desensitization, membrane trafficking, and pharmacological diversity, among others. Receptor dimerization/oligomerization is a challenging phenomenon to disentangle even in vitro and thus in vivo evidence for its functional significance requires employment of a variety of cutting-edge techniques. Nevertheless, the evidence for GPCR di/oligomerization at the physiological level is mounting and has begun to shed light on an intricate network of interactions that challenge the previous knowledge on how this family of receptors function. Here, we summarize the evidence for GPCR di/oligomerization in living organisms with a particular focus of their involvement in health and disease.",

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author = "Adolfo Rivero-M{\"u}ller and Jonas, {Kim Carol} and Hanyaloglu, {Aylin Carla} and Ilpo Huhtaniemi",

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AU - Rivero-Müller, Adolfo

AU - Jonas, Kim Carol

AU - Hanyaloglu, Aylin Carla

AU - Huhtaniemi, Ilpo

PY - 2013

Y1 - 2013

N2 - Initially considered as strict and rigid monomers, GPCRs have shown an ever-increasing flexibility in the number of intermolecular interactions they can participate in. Few rules can be applied to all members of this receptor superfamily, as the functional roles of resulting dimers or oligomers vary widely from biosynthesis, functional complementation, enhancement and control of signaling, positive and negative cooperativity, signal desensitization, membrane trafficking, and pharmacological diversity, among others. Receptor dimerization/oligomerization is a challenging phenomenon to disentangle even in vitro and thus in vivo evidence for its functional significance requires employment of a variety of cutting-edge techniques. Nevertheless, the evidence for GPCR di/oligomerization at the physiological level is mounting and has begun to shed light on an intricate network of interactions that challenge the previous knowledge on how this family of receptors function. Here, we summarize the evidence for GPCR di/oligomerization in living organisms with a particular focus of their involvement in health and disease.

AB - Initially considered as strict and rigid monomers, GPCRs have shown an ever-increasing flexibility in the number of intermolecular interactions they can participate in. Few rules can be applied to all members of this receptor superfamily, as the functional roles of resulting dimers or oligomers vary widely from biosynthesis, functional complementation, enhancement and control of signaling, positive and negative cooperativity, signal desensitization, membrane trafficking, and pharmacological diversity, among others. Receptor dimerization/oligomerization is a challenging phenomenon to disentangle even in vitro and thus in vivo evidence for its functional significance requires employment of a variety of cutting-edge techniques. Nevertheless, the evidence for GPCR di/oligomerization at the physiological level is mounting and has begun to shed light on an intricate network of interactions that challenge the previous knowledge on how this family of receptors function. Here, we summarize the evidence for GPCR di/oligomerization in living organisms with a particular focus of their involvement in health and disease.

KW - Animals

KW - Cells/metabolism

KW - Disease

KW - Health

KW - Humans

KW - Models, Molecular

KW - Protein Multimerization

KW - Receptors, G-Protein-Coupled/chemistry

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DO - 10.1016/B978-0-12-386931-9.00007-6

M3 - Review article

C2 - 23663969

SN - 1877-1173

VL - 117

SP - 163

EP - 185

JO - Progress in molecular biology and translational science

JF - Progress in molecular biology and translational science

ER -

Di/oligomerization of GPCRs-mechanisms and functional significance

Abstract

Keywords

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