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Protein kinase A directly phosphorylates metabotropic glutamate receptor 5 to modulate its function
KTH, School of Engineering Sciences (SCI), Applied Physics, Cell Physics.ORCID iD: 0000-0003-3402-9672
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2015 (English)In: Journal of Neurochemistry, ISSN 0022-3042, E-ISSN 1471-4159, Vol. 132, no 6, 677-686 p.Article in journal (Refereed) Published
Abstract [en]

Metabotropic glutamate receptor 5 (mGluR5) regulates excitatory post-synaptic signaling in the central nervous system (CNS) and is implicated in various CNS disorders. Protein kinase A (PKA) signaling is known to play a critical role in neuropsychiatric disorders such as Parkinson's disease, schizophrenia, and addiction. Dopamine signaling is known to modulate the properties of mGluR5 in a cAMP-and PKA-dependent manner, suggesting that mGluR5 may be a direct target for PKA. Our study identifies mGluR5 at Ser870 as a direct substrate for PKA phosphorylation and demonstrates that this phosphorylation plays a critical role in the PKA-mediated modulation of mGluR5 functions such as extracellular signal-regulated kinase phosphorylation and intracellular Ca2+ oscillations. The identification of the molecular mechanism by which PKA signaling modulates mGluR5-mediated cellular responses contributes to the understanding of the interaction between dopaminergic and glutamatergic neuronal signaling.

Place, publisher, year, edition, pages
2015. Vol. 132, no 6, 677-686 p.
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Biochemistry and Molecular Biology
URN: urn:nbn:se:kth:diva-164471DOI: 10.1111/jnc.13038ISI: 000351392800006PubMedID: 25639954ScopusID: 2-s2.0-84924586659OAI: diva2:806856

QC 20150422

Available from: 2015-04-22 Created: 2015-04-17 Last updated: 2015-04-22Bibliographically approved

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Zelenina, Marina
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