Comparative analysis of palmitoylation sites of serotonin (5‐HT) receptors in vertebrates
Abstract Background In the vertebrate central nervous system as well as in the periphery, serotonin, also known as 5‐hydroxytriptamine (5‐HT), function as a neurotransmitter, a hormone or a mitogen. 5‐HT receptors are composed of 7 family 5‐HT1‐7 receptors, comprising of 14 structurally and pharmaco...
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| Format: | Article |
| Language: | English |
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Wiley
2018-06-01
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| Series: | Neuropsychopharmacology Reports |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/npr2.12011 |
| _version_ | 1811301363611598848 |
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| author | Toshie Kaizuka Takashi Hayashi |
| author_facet | Toshie Kaizuka Takashi Hayashi |
| author_sort | Toshie Kaizuka |
| collection | DOAJ |
| description | Abstract Background In the vertebrate central nervous system as well as in the periphery, serotonin, also known as 5‐hydroxytriptamine (5‐HT), function as a neurotransmitter, a hormone or a mitogen. 5‐HT receptors are composed of 7 family 5‐HT1‐7 receptors, comprising of 14 structurally and pharmacologically distinct 5‐HT receptor subtypes. Previous experimental studies showed that mouse 5‐HT1A, 5‐HT4 and 5‐HT7 receptors are regulated by post‐translational protein palmitoylation, the reversible attachment of the lipid palmitate to intracellular cysteine residues. Here, we further focused on conservation of these putative palmitoylation sites found in vertebrate 5‐HT receptor orthologs. Methods and Results Analysis of sequence databases provides evidence to suggest that palmitoylation sites of these 5‐HT receptors have been extremely conserved in the vertebrate lineages from jawless fishes to human, in spite of the divergence of 5‐HT1A, 5‐HT4 or 5‐HT7 receptors full‐length amino acid sequences during molecular evolution. Conclusion Our findings mean that dynamic regulation of 5‐HT receptors made possible by reversible post‐translational protein palmitoylation may be critical for refined functions of the vertebrate serotonergic systems. |
| first_indexed | 2024-04-13T07:07:33Z |
| format | Article |
| id | doaj.art-40eac666e2274df9b67bb76028252cd9 |
| institution | Directory Open Access Journal |
| issn | 2574-173X |
| language | English |
| last_indexed | 2024-04-13T07:07:33Z |
| publishDate | 2018-06-01 |
| publisher | Wiley |
| record_format | Article |
| series | Neuropsychopharmacology Reports |
| spelling | doaj.art-40eac666e2274df9b67bb76028252cd92022-12-22T02:56:57ZengWileyNeuropsychopharmacology Reports2574-173X2018-06-01382758510.1002/npr2.12011Comparative analysis of palmitoylation sites of serotonin (5‐HT) receptors in vertebratesToshie Kaizuka0Takashi Hayashi1Section of Cellular Biochemistry Department of Biochemistry and Cellular Biology National Institute of Neuroscience National Center of Neurology and Psychiatry (NCNP) Tokyo JapanSection of Cellular Biochemistry Department of Biochemistry and Cellular Biology National Institute of Neuroscience National Center of Neurology and Psychiatry (NCNP) Tokyo JapanAbstract Background In the vertebrate central nervous system as well as in the periphery, serotonin, also known as 5‐hydroxytriptamine (5‐HT), function as a neurotransmitter, a hormone or a mitogen. 5‐HT receptors are composed of 7 family 5‐HT1‐7 receptors, comprising of 14 structurally and pharmacologically distinct 5‐HT receptor subtypes. Previous experimental studies showed that mouse 5‐HT1A, 5‐HT4 and 5‐HT7 receptors are regulated by post‐translational protein palmitoylation, the reversible attachment of the lipid palmitate to intracellular cysteine residues. Here, we further focused on conservation of these putative palmitoylation sites found in vertebrate 5‐HT receptor orthologs. Methods and Results Analysis of sequence databases provides evidence to suggest that palmitoylation sites of these 5‐HT receptors have been extremely conserved in the vertebrate lineages from jawless fishes to human, in spite of the divergence of 5‐HT1A, 5‐HT4 or 5‐HT7 receptors full‐length amino acid sequences during molecular evolution. Conclusion Our findings mean that dynamic regulation of 5‐HT receptors made possible by reversible post‐translational protein palmitoylation may be critical for refined functions of the vertebrate serotonergic systems.https://doi.org/10.1002/npr2.120115‐hydroxytryptamineorthologspost‐translational protein palmitoylationreceptorserotoninvertebrate |
| spellingShingle | Toshie Kaizuka Takashi Hayashi Comparative analysis of palmitoylation sites of serotonin (5‐HT) receptors in vertebrates Neuropsychopharmacology Reports 5‐hydroxytryptamine orthologs post‐translational protein palmitoylation receptor serotonin vertebrate |
| title | Comparative analysis of palmitoylation sites of serotonin (5‐HT) receptors in vertebrates |
| title_full | Comparative analysis of palmitoylation sites of serotonin (5‐HT) receptors in vertebrates |
| title_fullStr | Comparative analysis of palmitoylation sites of serotonin (5‐HT) receptors in vertebrates |
| title_full_unstemmed | Comparative analysis of palmitoylation sites of serotonin (5‐HT) receptors in vertebrates |
| title_short | Comparative analysis of palmitoylation sites of serotonin (5‐HT) receptors in vertebrates |
| title_sort | comparative analysis of palmitoylation sites of serotonin 5 ht receptors in vertebrates |
| topic | 5‐hydroxytryptamine orthologs post‐translational protein palmitoylation receptor serotonin vertebrate |
| url | https://doi.org/10.1002/npr2.12011 |
| work_keys_str_mv | AT toshiekaizuka comparativeanalysisofpalmitoylationsitesofserotonin5htreceptorsinvertebrates AT takashihayashi comparativeanalysisofpalmitoylationsitesofserotonin5htreceptorsinvertebrates |