author_facet Von Buchholtz, Lars
Elischer, Andrea
Tareilus, Erwin
Gouka, Robin
Kaiser, Carmen
Breer, Heinz
Conzelmann, Sidonie
Von Buchholtz, Lars
Elischer, Andrea
Tareilus, Erwin
Gouka, Robin
Kaiser, Carmen
Breer, Heinz
Conzelmann, Sidonie
author Von Buchholtz, Lars
Elischer, Andrea
Tareilus, Erwin
Gouka, Robin
Kaiser, Carmen
Breer, Heinz
Conzelmann, Sidonie
spellingShingle Von Buchholtz, Lars
Elischer, Andrea
Tareilus, Erwin
Gouka, Robin
Kaiser, Carmen
Breer, Heinz
Conzelmann, Sidonie
European Journal of Neuroscience
RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
General Neuroscience
author_sort von buchholtz, lars
spelling Von Buchholtz, Lars Elischer, Andrea Tareilus, Erwin Gouka, Robin Kaiser, Carmen Breer, Heinz Conzelmann, Sidonie 0953-816X 1460-9568 Wiley General Neuroscience http://dx.doi.org/10.1111/j.1460-9568.2004.03257.x <jats:title>Abstract</jats:title><jats:p>G‐protein‐mediated signalling processes are involved in sweet and bitter taste transduction. In particular, the G protein α‐subunit gustducin has been implicated in these processes. One of the limiting factors for the time‐course of cellular responses induced by tastants is therefore the intrinsic GTPase activity of α‐gustducin, which determines the lifetime of the active G protein complex. In several signalling systems specific ‘regulator of G protein signalling’ (RGS) proteins accelerate the GTPase activity of G protein α‐subunits. Using differential screening approaches, we have identified a novel RGS protein termed RGS21, which represents the smallest known member of this protein family. Reverse transcription polymerase chain reaction and <jats:italic>in situ</jats:italic> hybridization experiments demonstrated that RGS21 is expressed selectively in taste tissue where it is found in a subpopulation of sensory cells. Furthermore, it is coexpressed in individual taste cells with bitter and sweet transduction components including α‐gustducin, phospholipase Cβ2, T1R2/T1R3 sweet taste receptors and T2R bitter taste receptors. <jats:italic>In vitro</jats:italic> binding assays demonstrate that RGS21 binds α‐gustducin in a conformation‐dependent manner and has the potential to interact with the same Gα subtypes as T1R receptors. These results suggest that RGS21 could play a regulatory role in bitter as well as sweet taste transduction processes.</jats:p> RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells European Journal of Neuroscience
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title RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_unstemmed RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_full RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_fullStr RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_full_unstemmed RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_short RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_sort rgs21 is a novel regulator of g protein signalling selectively expressed in subpopulations of taste bud cells
topic General Neuroscience
url http://dx.doi.org/10.1111/j.1460-9568.2004.03257.x
publishDate 2004
physical 1535-1544
description <jats:title>Abstract</jats:title><jats:p>G‐protein‐mediated signalling processes are involved in sweet and bitter taste transduction. In particular, the G protein α‐subunit gustducin has been implicated in these processes. One of the limiting factors for the time‐course of cellular responses induced by tastants is therefore the intrinsic GTPase activity of α‐gustducin, which determines the lifetime of the active G protein complex. In several signalling systems specific ‘regulator of G protein signalling’ (RGS) proteins accelerate the GTPase activity of G protein α‐subunits. Using differential screening approaches, we have identified a novel RGS protein termed RGS21, which represents the smallest known member of this protein family. Reverse transcription polymerase chain reaction and <jats:italic>in situ</jats:italic> hybridization experiments demonstrated that RGS21 is expressed selectively in taste tissue where it is found in a subpopulation of sensory cells. Furthermore, it is coexpressed in individual taste cells with bitter and sweet transduction components including α‐gustducin, phospholipase Cβ2, T1R2/T1R3 sweet taste receptors and T2R bitter taste receptors. <jats:italic>In vitro</jats:italic> binding assays demonstrate that RGS21 binds α‐gustducin in a conformation‐dependent manner and has the potential to interact with the same Gα subtypes as T1R receptors. These results suggest that RGS21 could play a regulatory role in bitter as well as sweet taste transduction processes.</jats:p>
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author Von Buchholtz, Lars, Elischer, Andrea, Tareilus, Erwin, Gouka, Robin, Kaiser, Carmen, Breer, Heinz, Conzelmann, Sidonie
author_facet Von Buchholtz, Lars, Elischer, Andrea, Tareilus, Erwin, Gouka, Robin, Kaiser, Carmen, Breer, Heinz, Conzelmann, Sidonie, Von Buchholtz, Lars, Elischer, Andrea, Tareilus, Erwin, Gouka, Robin, Kaiser, Carmen, Breer, Heinz, Conzelmann, Sidonie
author_sort von buchholtz, lars
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description <jats:title>Abstract</jats:title><jats:p>G‐protein‐mediated signalling processes are involved in sweet and bitter taste transduction. In particular, the G protein α‐subunit gustducin has been implicated in these processes. One of the limiting factors for the time‐course of cellular responses induced by tastants is therefore the intrinsic GTPase activity of α‐gustducin, which determines the lifetime of the active G protein complex. In several signalling systems specific ‘regulator of G protein signalling’ (RGS) proteins accelerate the GTPase activity of G protein α‐subunits. Using differential screening approaches, we have identified a novel RGS protein termed RGS21, which represents the smallest known member of this protein family. Reverse transcription polymerase chain reaction and <jats:italic>in situ</jats:italic> hybridization experiments demonstrated that RGS21 is expressed selectively in taste tissue where it is found in a subpopulation of sensory cells. Furthermore, it is coexpressed in individual taste cells with bitter and sweet transduction components including α‐gustducin, phospholipase Cβ2, T1R2/T1R3 sweet taste receptors and T2R bitter taste receptors. <jats:italic>In vitro</jats:italic> binding assays demonstrate that RGS21 binds α‐gustducin in a conformation‐dependent manner and has the potential to interact with the same Gα subtypes as T1R receptors. These results suggest that RGS21 could play a regulatory role in bitter as well as sweet taste transduction processes.</jats:p>
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spelling Von Buchholtz, Lars Elischer, Andrea Tareilus, Erwin Gouka, Robin Kaiser, Carmen Breer, Heinz Conzelmann, Sidonie 0953-816X 1460-9568 Wiley General Neuroscience http://dx.doi.org/10.1111/j.1460-9568.2004.03257.x <jats:title>Abstract</jats:title><jats:p>G‐protein‐mediated signalling processes are involved in sweet and bitter taste transduction. In particular, the G protein α‐subunit gustducin has been implicated in these processes. One of the limiting factors for the time‐course of cellular responses induced by tastants is therefore the intrinsic GTPase activity of α‐gustducin, which determines the lifetime of the active G protein complex. In several signalling systems specific ‘regulator of G protein signalling’ (RGS) proteins accelerate the GTPase activity of G protein α‐subunits. Using differential screening approaches, we have identified a novel RGS protein termed RGS21, which represents the smallest known member of this protein family. Reverse transcription polymerase chain reaction and <jats:italic>in situ</jats:italic> hybridization experiments demonstrated that RGS21 is expressed selectively in taste tissue where it is found in a subpopulation of sensory cells. Furthermore, it is coexpressed in individual taste cells with bitter and sweet transduction components including α‐gustducin, phospholipase Cβ2, T1R2/T1R3 sweet taste receptors and T2R bitter taste receptors. <jats:italic>In vitro</jats:italic> binding assays demonstrate that RGS21 binds α‐gustducin in a conformation‐dependent manner and has the potential to interact with the same Gα subtypes as T1R receptors. These results suggest that RGS21 could play a regulatory role in bitter as well as sweet taste transduction processes.</jats:p> RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells European Journal of Neuroscience
spellingShingle Von Buchholtz, Lars, Elischer, Andrea, Tareilus, Erwin, Gouka, Robin, Kaiser, Carmen, Breer, Heinz, Conzelmann, Sidonie, European Journal of Neuroscience, RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells, General Neuroscience
title RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_full RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_fullStr RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_full_unstemmed RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_short RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
title_sort rgs21 is a novel regulator of g protein signalling selectively expressed in subpopulations of taste bud cells
title_unstemmed RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
topic General Neuroscience
url http://dx.doi.org/10.1111/j.1460-9568.2004.03257.x