期刊
MOLECULAR PHARMACOLOGY
卷 65, 期 1, 页码 252-256出版社
AMER SOC PHARMACOLOGY EXPERIMENTAL THERAPEUTICS
DOI: 10.1124/mol.65.1.252
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资金
- NIGMS NIH HHS [GM07623] Funding Source: Medline
- NIMH NIH HHS [MH34007] Funding Source: Medline
- NINDS NIH HHS [NS35891] Funding Source: Medline
- NATIONAL INSTITUTE OF MENTAL HEALTH [R01MH034007, R37MH034007] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS035891] Funding Source: NIH RePORTER
The human serotonin 5-HT2C receptor undergoes adenosine-to-inosine RNA editing at five positions, generating multiple receptor isoforms with altered G-protein coupling properties. In the current study, we demonstrate that RNA editing regulates the pattern of intracellular signaling. The non-edited human 5-HT2C receptor isoform INI activates phospholipase D via the G(13) heterotrimer G-protein. We present evidence that transactivation of the small G-protein RhoA is required for phospholipase D activation. In contrast, neither transactivation of RhoA nor phospholipase D activation was detected in cells expressing the fully edited VGV isoform. The ability to activate phospholipase C is also reduced in VGV-expressing cells, but not to the extent found for the phospholipase D signal. We conclude that RNA editing represents a novel mechanism for regulating 5-HT2C receptor signaling to pathways linked to actin cytoskeletal organization and regulated exocytosis.
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