author_facet Wachten, Sebastian
Schlenstedt, Jana
Gauss, Renate
Baumann, Arnd
Wachten, Sebastian
Schlenstedt, Jana
Gauss, Renate
Baumann, Arnd
author Wachten, Sebastian
Schlenstedt, Jana
Gauss, Renate
Baumann, Arnd
spellingShingle Wachten, Sebastian
Schlenstedt, Jana
Gauss, Renate
Baumann, Arnd
Journal of Neurochemistry
Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
Cellular and Molecular Neuroscience
Biochemistry
author_sort wachten, sebastian
spelling Wachten, Sebastian Schlenstedt, Jana Gauss, Renate Baumann, Arnd 0022-3042 1471-4159 Wiley Cellular and Molecular Neuroscience Biochemistry http://dx.doi.org/10.1111/j.1471-4159.2006.03666.x <jats:title>Abstract</jats:title><jats:p>Cyclic AMP (cAMP) serves as an important messenger in virtually all organisms. In the honeybee (<jats:italic>Apis mellifera</jats:italic>), cAMP‐dependent signal transduction has been implicated in behavioural processes as well as in learning and memory. Key components of cAMP‐signalling cascades are adenylyl cyclases. However, the molecular identities and biochemical properties of adenylyl cyclases are completely unknown in the honeybee. We have cloned a cDNA (Am<jats:italic>ac</jats:italic>3) from honeybee brain that encodes a membrane‐bound adenylyl cyclase. The Am<jats:italic>ac</jats:italic>3 gene is an orthologue of the <jats:italic>Drosophila ac</jats:italic>39E gene. The corresponding proteins share an overall amino acid similarity of approximately 62%. Phylogenetically, AmAC3 belongs to group 1 adenylyl cyclases. Heterologously expressed AmAC3 displays basal enzymatic activity and efficient coupling to endogenous G protein signalling pathways. Stimulation of β‐adrenergic receptors induces AmAC3 activity with an EC<jats:sub>50</jats:sub> of about 3.1 µ<jats:sc>m</jats:sc>. Enzymatic activity is also increased by forskolin (EC<jats:sub>50</jats:sub> approximately 15 µ<jats:sc>m</jats:sc>), a specific agonist of membrane‐bound adenylyl cyclases. Similar to certain biogenic amine receptor genes of the honeybee, Am<jats:italic>ac</jats:italic>3 transcripts are expressed in many somata of the brain, especially in mushroom body neurones. These results suggest that the enzyme serves in biogenic amine signal transduction cascades and in higher brain functions that contribute to learning and memory of the bee.</jats:p> Molecular identification and functional characterization of an adenylyl cyclase from the honeybee Journal of Neurochemistry
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source_id 49
title Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_unstemmed Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_full Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_fullStr Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_full_unstemmed Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_short Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_sort molecular identification and functional characterization of an adenylyl cyclase from the honeybee
topic Cellular and Molecular Neuroscience
Biochemistry
url http://dx.doi.org/10.1111/j.1471-4159.2006.03666.x
publishDate 2006
physical 1580-1590
description <jats:title>Abstract</jats:title><jats:p>Cyclic AMP (cAMP) serves as an important messenger in virtually all organisms. In the honeybee (<jats:italic>Apis mellifera</jats:italic>), cAMP‐dependent signal transduction has been implicated in behavioural processes as well as in learning and memory. Key components of cAMP‐signalling cascades are adenylyl cyclases. However, the molecular identities and biochemical properties of adenylyl cyclases are completely unknown in the honeybee. We have cloned a cDNA (Am<jats:italic>ac</jats:italic>3) from honeybee brain that encodes a membrane‐bound adenylyl cyclase. The Am<jats:italic>ac</jats:italic>3 gene is an orthologue of the <jats:italic>Drosophila ac</jats:italic>39E gene. The corresponding proteins share an overall amino acid similarity of approximately 62%. Phylogenetically, AmAC3 belongs to group 1 adenylyl cyclases. Heterologously expressed AmAC3 displays basal enzymatic activity and efficient coupling to endogenous G protein signalling pathways. Stimulation of β‐adrenergic receptors induces AmAC3 activity with an EC<jats:sub>50</jats:sub> of about 3.1 µ<jats:sc>m</jats:sc>. Enzymatic activity is also increased by forskolin (EC<jats:sub>50</jats:sub> approximately 15 µ<jats:sc>m</jats:sc>), a specific agonist of membrane‐bound adenylyl cyclases. Similar to certain biogenic amine receptor genes of the honeybee, Am<jats:italic>ac</jats:italic>3 transcripts are expressed in many somata of the brain, especially in mushroom body neurones. These results suggest that the enzyme serves in biogenic amine signal transduction cascades and in higher brain functions that contribute to learning and memory of the bee.</jats:p>
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author Wachten, Sebastian, Schlenstedt, Jana, Gauss, Renate, Baumann, Arnd
author_facet Wachten, Sebastian, Schlenstedt, Jana, Gauss, Renate, Baumann, Arnd, Wachten, Sebastian, Schlenstedt, Jana, Gauss, Renate, Baumann, Arnd
author_sort wachten, sebastian
container_issue 6
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description <jats:title>Abstract</jats:title><jats:p>Cyclic AMP (cAMP) serves as an important messenger in virtually all organisms. In the honeybee (<jats:italic>Apis mellifera</jats:italic>), cAMP‐dependent signal transduction has been implicated in behavioural processes as well as in learning and memory. Key components of cAMP‐signalling cascades are adenylyl cyclases. However, the molecular identities and biochemical properties of adenylyl cyclases are completely unknown in the honeybee. We have cloned a cDNA (Am<jats:italic>ac</jats:italic>3) from honeybee brain that encodes a membrane‐bound adenylyl cyclase. The Am<jats:italic>ac</jats:italic>3 gene is an orthologue of the <jats:italic>Drosophila ac</jats:italic>39E gene. The corresponding proteins share an overall amino acid similarity of approximately 62%. Phylogenetically, AmAC3 belongs to group 1 adenylyl cyclases. Heterologously expressed AmAC3 displays basal enzymatic activity and efficient coupling to endogenous G protein signalling pathways. Stimulation of β‐adrenergic receptors induces AmAC3 activity with an EC<jats:sub>50</jats:sub> of about 3.1 µ<jats:sc>m</jats:sc>. Enzymatic activity is also increased by forskolin (EC<jats:sub>50</jats:sub> approximately 15 µ<jats:sc>m</jats:sc>), a specific agonist of membrane‐bound adenylyl cyclases. Similar to certain biogenic amine receptor genes of the honeybee, Am<jats:italic>ac</jats:italic>3 transcripts are expressed in many somata of the brain, especially in mushroom body neurones. These results suggest that the enzyme serves in biogenic amine signal transduction cascades and in higher brain functions that contribute to learning and memory of the bee.</jats:p>
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spelling Wachten, Sebastian Schlenstedt, Jana Gauss, Renate Baumann, Arnd 0022-3042 1471-4159 Wiley Cellular and Molecular Neuroscience Biochemistry http://dx.doi.org/10.1111/j.1471-4159.2006.03666.x <jats:title>Abstract</jats:title><jats:p>Cyclic AMP (cAMP) serves as an important messenger in virtually all organisms. In the honeybee (<jats:italic>Apis mellifera</jats:italic>), cAMP‐dependent signal transduction has been implicated in behavioural processes as well as in learning and memory. Key components of cAMP‐signalling cascades are adenylyl cyclases. However, the molecular identities and biochemical properties of adenylyl cyclases are completely unknown in the honeybee. We have cloned a cDNA (Am<jats:italic>ac</jats:italic>3) from honeybee brain that encodes a membrane‐bound adenylyl cyclase. The Am<jats:italic>ac</jats:italic>3 gene is an orthologue of the <jats:italic>Drosophila ac</jats:italic>39E gene. The corresponding proteins share an overall amino acid similarity of approximately 62%. Phylogenetically, AmAC3 belongs to group 1 adenylyl cyclases. Heterologously expressed AmAC3 displays basal enzymatic activity and efficient coupling to endogenous G protein signalling pathways. Stimulation of β‐adrenergic receptors induces AmAC3 activity with an EC<jats:sub>50</jats:sub> of about 3.1 µ<jats:sc>m</jats:sc>. Enzymatic activity is also increased by forskolin (EC<jats:sub>50</jats:sub> approximately 15 µ<jats:sc>m</jats:sc>), a specific agonist of membrane‐bound adenylyl cyclases. Similar to certain biogenic amine receptor genes of the honeybee, Am<jats:italic>ac</jats:italic>3 transcripts are expressed in many somata of the brain, especially in mushroom body neurones. These results suggest that the enzyme serves in biogenic amine signal transduction cascades and in higher brain functions that contribute to learning and memory of the bee.</jats:p> Molecular identification and functional characterization of an adenylyl cyclase from the honeybee Journal of Neurochemistry
spellingShingle Wachten, Sebastian, Schlenstedt, Jana, Gauss, Renate, Baumann, Arnd, Journal of Neurochemistry, Molecular identification and functional characterization of an adenylyl cyclase from the honeybee, Cellular and Molecular Neuroscience, Biochemistry
title Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_full Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_fullStr Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_full_unstemmed Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_short Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_sort molecular identification and functional characterization of an adenylyl cyclase from the honeybee
title_unstemmed Molecular identification and functional characterization of an adenylyl cyclase from the honeybee
topic Cellular and Molecular Neuroscience, Biochemistry
url http://dx.doi.org/10.1111/j.1471-4159.2006.03666.x