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The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signaling
- Source :
- Science Signaling. 8
- Publication Year :
- 2015
- Publisher :
- American Association for the Advancement of Science (AAAS), 2015.
-
Abstract
- Protein arginine methylation regulates diverse functions of eukaryotic cells, including gene expression, the DNA damage response, and circadian rhythms. We showed that arginine residues within the third intracellular loop of the human D2 dopamine receptor, which are conserved in the DOP-3 receptor in the nematode Caenorhabditis elegans , were methylated by protein arginine methyltransferase 5 (PRMT5). By mutating these arginine residues, we further showed that their methylation enhanced the D2 receptor–mediated inhibition of cyclic adenosine monophosphate (cAMP) signaling in cultured human embryonic kidney (HEK) 293T cells. Analysis of prmt-5 –deficient worms indicated that methylation promoted the dopamine-mediated modulation of chemosensory and locomotory behaviors in C. elegans through the DOP-3 receptor. In addition to delineating a previously uncharacterized means of regulating GPCR (heterotrimeric guanine nucleotide–binding protein–coupled receptor) signaling, these findings may lead to the development of a new class of pharmacological therapies that modulate GPCR signaling by changing the methylation status of these key proteins.
- Subjects :
- Octanols
Protein-Arginine N-Methyltransferases
Arginine
Dopamine
Amino Acid Motifs
Molecular Sequence Data
Biology
Methylation
Biochemistry
Article
Receptors, G-Protein-Coupled
Animals, Genetically Modified
chemistry.chemical_compound
Animals
Humans
Cyclic adenosine monophosphate
Amino Acid Sequence
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Molecular Biology
Conserved Sequence
G protein-coupled receptor
Sequence Homology, Amino Acid
Receptors, Dopamine D2
Protein arginine methyltransferase 5
HEK 293 cells
Computational Biology
Cell Biology
HEK293 Cells
chemistry
Odorants
Signal transduction
Locomotion
Signal Transduction
Subjects
Details
- ISSN :
- 19379145 and 19450877
- Volume :
- 8
- Database :
- OpenAIRE
- Journal :
- Science Signaling
- Accession number :
- edsair.doi.dedup.....a2374febc461c67c2bdd59d0d365bac5