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dc.contributor.authorUematsu, Ken
dc.contributor.authorHeiman, Myriam
dc.contributor.authorZelenina, Marina
dc.contributor.authorPadovan, Julio
dc.contributor.authorChait, Brian T.
dc.contributor.authorAperia, Anita
dc.contributor.authorNishi, Akinori
dc.contributor.authorGreengard, Paul
dc.date.accessioned2016-05-09T17:37:06Z
dc.date.available2016-05-09T17:37:06Z
dc.date.issued2015-03
dc.date.submitted2014-12
dc.identifier.issn00223042
dc.identifier.issn1471-4159
dc.identifier.urihttp://hdl.handle.net/1721.1/102444
dc.description.abstractMetabotropic 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 Ca[superscript 2+] 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. We identified serine residue 870 (S870) in metabotropic glutamate receptor 5 (mGluR5) as a direct substrate for protein kinase A (PKA). The phosphorylation of this site regulates the ability of mGluR5 to induce extracellular signal-regulated kinase (ERK) phosphorylation and intracellular Ca[superscript 2+] oscillations. This study provides a direct molecular mechanism by which PKA signaling interacts with glutamate neurotransmission.en_US
dc.language.isoen_US
dc.publisherWiley Blackwellen_US
dc.relation.isversionofhttp://dx.doi.org/10.1111/jnc.13038en_US
dc.rightsCreative Commons Attribution-Noncommercial-Share Alikeen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/en_US
dc.sourcePMCen_US
dc.titleProtein kinase A directly phosphorylates metabotropic glutamate receptor 5 to modulate its functionen_US
dc.typeArticleen_US
dc.identifier.citationUematsu, Ken, Myriam Heiman, Marina Zelenina, Julio Padovan, Brian T. Chait, Anita Aperia, Akinori Nishi, and Paul Greengard. “Protein Kinase A Directly Phosphorylates Metabotropic Glutamate Receptor 5 to Modulate Its Function.” Journal of Neurochemistry 132, no. 6 (March 2015): 677–686.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Brain and Cognitive Sciencesen_US
dc.contributor.departmentPicower Institute for Learning and Memoryen_US
dc.contributor.mitauthorHeiman, Myriamen_US
dc.relation.journalJournal of Neurochemistryen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsUematsu, Ken; Heiman, Myriam; Zelenina, Marina; Padovan, Julio; Chait, Brian T.; Aperia, Anita; Nishi, Akinori; Greengard, Paulen_US
dc.identifier.orcidhttps://orcid.org/0000-0002-6365-8673
mit.licenseOPEN_ACCESS_POLICYen_US


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