Using cAMP Sensors to Study Cardiac Nanodomains

3′,5′-cyclic adenosine monophosphate (cAMP) signalling plays a major role in the cardiac myocyte response to extracellular stimulation by hormones and neurotransmitters. In recent years, evidence has accumulated demonstrating that the cAMP response to different extracellular agonists is not uniform:...

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Main Authors: Katharina Schleicher, Manuela Zaccolo
Format: Article
Language:English
Published: MDPI AG 2018-03-01
Series:Journal of Cardiovascular Development and Disease
Subjects:
Online Access:http://www.mdpi.com/2308-3425/5/1/17
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spelling doaj-c2013966d2a642328ed7f69c9b9e62e12020-11-24T22:04:07ZengMDPI AGJournal of Cardiovascular Development and Disease2308-34252018-03-01511710.3390/jcdd5010017jcdd5010017Using cAMP Sensors to Study Cardiac NanodomainsKatharina Schleicher0Manuela Zaccolo1Department of Physiology, Anatomy and Genetics, University of Oxford, Sherrington Building, South Parks Road, Oxford OX1 3PT, UKDepartment of Physiology, Anatomy and Genetics, University of Oxford, Sherrington Building, South Parks Road, Oxford OX1 3PT, UK3′,5′-cyclic adenosine monophosphate (cAMP) signalling plays a major role in the cardiac myocyte response to extracellular stimulation by hormones and neurotransmitters. In recent years, evidence has accumulated demonstrating that the cAMP response to different extracellular agonists is not uniform: depending on the stimulus, cAMP signals of different amplitudes and kinetics are generated in different subcellular compartments, eliciting defined physiological effects. In this review, we focus on how real-time imaging using fluorescence resonance energy transfer (FRET)-based reporters has provided mechanistic insight into the compartmentalisation of the cAMP signalling pathway and allowed for the precise definition of the regulation and function of subcellular cAMP nanodomains.http://www.mdpi.com/2308-3425/5/1/173′,5′-cyclic adenosine monophosphateprotein kinase Afluorescence resonance energy transferreal-time imagingcompartmentalisationsignallingcardiac biologyphosphodiesterasesA kinase anchoring proteins
collection DOAJ
language English
format Article
sources DOAJ
author Katharina Schleicher
Manuela Zaccolo
spellingShingle Katharina Schleicher
Manuela Zaccolo
Using cAMP Sensors to Study Cardiac Nanodomains
Journal of Cardiovascular Development and Disease
3′,5′-cyclic adenosine monophosphate
protein kinase A
fluorescence resonance energy transfer
real-time imaging
compartmentalisation
signalling
cardiac biology
phosphodiesterases
A kinase anchoring proteins
author_facet Katharina Schleicher
Manuela Zaccolo
author_sort Katharina Schleicher
title Using cAMP Sensors to Study Cardiac Nanodomains
title_short Using cAMP Sensors to Study Cardiac Nanodomains
title_full Using cAMP Sensors to Study Cardiac Nanodomains
title_fullStr Using cAMP Sensors to Study Cardiac Nanodomains
title_full_unstemmed Using cAMP Sensors to Study Cardiac Nanodomains
title_sort using camp sensors to study cardiac nanodomains
publisher MDPI AG
series Journal of Cardiovascular Development and Disease
issn 2308-3425
publishDate 2018-03-01
description 3′,5′-cyclic adenosine monophosphate (cAMP) signalling plays a major role in the cardiac myocyte response to extracellular stimulation by hormones and neurotransmitters. In recent years, evidence has accumulated demonstrating that the cAMP response to different extracellular agonists is not uniform: depending on the stimulus, cAMP signals of different amplitudes and kinetics are generated in different subcellular compartments, eliciting defined physiological effects. In this review, we focus on how real-time imaging using fluorescence resonance energy transfer (FRET)-based reporters has provided mechanistic insight into the compartmentalisation of the cAMP signalling pathway and allowed for the precise definition of the regulation and function of subcellular cAMP nanodomains.
topic 3′,5′-cyclic adenosine monophosphate
protein kinase A
fluorescence resonance energy transfer
real-time imaging
compartmentalisation
signalling
cardiac biology
phosphodiesterases
A kinase anchoring proteins
url http://www.mdpi.com/2308-3425/5/1/17
work_keys_str_mv AT katharinaschleicher usingcampsensorstostudycardiacnanodomains
AT manuelazaccolo usingcampsensorstostudycardiacnanodomains
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