| pubmed-article:21113197 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21113197 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:21113197 | lifeskim:mentions | umls-concept:C0034826 | lld:lifeskim |
| pubmed-article:21113197 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:21113197 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:21113197 | pubmed:dateCreated | 2010-11-29 | lld:pubmed |
| pubmed-article:21113197 | pubmed:abstractText | Protein-protein interactions represent an important mechanism for posttranslational modifications of protein expression and function. In brain cells, surface-expressed and membrane-bound neurotransmitter receptors are common proteins that undergo dynamic protein-protein interactions between their intracellular domains and submembranous regulatory proteins. Recently, the G?(i/o)-coupled muscarinic M4 receptor (M4R) has been revealed to be one of these receptors. Through direct interaction with the intracellular loops or C-terminal tails of M4Rs, M4R interacting proteins (M4RIPs) vigorously regulate the efficacy of M4R signaling. A synapse-enriched protein kinase, Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), exemplifies a prototype model of M4RIPs, and is capable of binding to the second intracellular loop of M4Rs. Through an activity- and phosphorylation-dependent mechanism, CaMKII potentiates the M4R/G?(i/o)-mediated inhibition of M4R efficacy in inhibiting adenylyl cyclase and cAMP production. In striatal neurons where M4Rs are most abundantly expressed, M4RIPs dynamically control M4R activity to maintain a proper cholinergic tone in these neurons. This is critical for maintaining the acetylcholine-dopamine balance in the basal ganglia, which determines the behavioral responsiveness to dopamine stimulation by psychostimulants. | lld:pubmed |
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| pubmed-article:21113197 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21113197 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21113197 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21113197 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21113197 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21113197 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21113197 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:21113197 | pubmed:issn | 1995-8218 | lld:pubmed |
| pubmed-article:21113197 | pubmed:author | pubmed-author:WangJohn QJQ | lld:pubmed |
| pubmed-article:21113197 | pubmed:author | pubmed-author:MaoLi-MinLM | lld:pubmed |
| pubmed-article:21113197 | pubmed:author | pubmed-author:GuoMing-LeiML | lld:pubmed |
| pubmed-article:21113197 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21113197 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:21113197 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21113197 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21113197 | pubmed:pagination | 469-73 | lld:pubmed |
| pubmed-article:21113197 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:21113197 | pubmed:meshHeading | pubmed-meshheading:21113197... | lld:pubmed |
| pubmed-article:21113197 | pubmed:meshHeading | pubmed-meshheading:21113197... | lld:pubmed |
| pubmed-article:21113197 | pubmed:meshHeading | pubmed-meshheading:21113197... | lld:pubmed |
| pubmed-article:21113197 | pubmed:meshHeading | pubmed-meshheading:21113197... | lld:pubmed |
| pubmed-article:21113197 | pubmed:meshHeading | pubmed-meshheading:21113197... | lld:pubmed |
| pubmed-article:21113197 | pubmed:meshHeading | pubmed-meshheading:21113197... | lld:pubmed |
| pubmed-article:21113197 | pubmed:meshHeading | pubmed-meshheading:21113197... | lld:pubmed |
| pubmed-article:21113197 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:21113197 | pubmed:articleTitle | Modulation of M4 muscarinic acetylcholine receptors by interacting proteins. | lld:pubmed |
| pubmed-article:21113197 | pubmed:affiliation | Department of Basic Medical Science, University of Missouri-Kansas City School of Medicine, Kansas City, MO 64108, USA. wangjq@umkc.edu | lld:pubmed |
| pubmed-article:21113197 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21113197 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:21113197 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21113197 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
