| pubmed-article:10995758 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10995758 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:10995758 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:10995758 | lifeskim:mentions | umls-concept:C0080093 | lld:lifeskim |
| pubmed-article:10995758 | lifeskim:mentions | umls-concept:C0900627 | lld:lifeskim |
| pubmed-article:10995758 | lifeskim:mentions | umls-concept:C1333226 | lld:lifeskim |
| pubmed-article:10995758 | lifeskim:mentions | umls-concept:C1705335 | lld:lifeskim |
| pubmed-article:10995758 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:10995758 | lifeskim:mentions | umls-concept:C1372999 | lld:lifeskim |
| pubmed-article:10995758 | lifeskim:mentions | umls-concept:C2248016 | lld:lifeskim |
| pubmed-article:10995758 | lifeskim:mentions | umls-concept:C0234112 | lld:lifeskim |
| pubmed-article:10995758 | pubmed:issue | 49 | lld:pubmed |
| pubmed-article:10995758 | pubmed:dateCreated | 2001-1-18 | lld:pubmed |
| pubmed-article:10995758 | pubmed:abstractText | The beta(1)-adrenergic receptor (beta(1)AR) is the most abundant subtype of beta-adrenergic receptor in the mammalian brain and is known to potently regulate synaptic plasticity. To search for potential neuronal beta(1)AR-interacting proteins, we screened a rat brain cDNA library using the beta(1)AR carboxyl terminus (beta(1)AR-CT) as bait in the yeast two-hybrid system. These screens identified PSD-95, a multiple PDZ domain-containing scaffolding protein, as a specific binding partner of the beta(1)AR-CT. This interaction was confirmed by in vitro fusion protein pull-down and blot overlay experiments, which demonstrated that the beta(1)AR-CT binds specifically to the third PDZ domain of PSD-95. Furthermore, the full-length beta(1)AR associates with PSD-95 in cells, as determined by co-immunoprecipitation experiments and immunofluorescence co-localization studies. The interaction between beta(1)AR and PSD-95 is mediated by the last few amino acids of the beta(1)AR, and mutation of the beta(1)AR carboxyl terminus eliminated the binding and disrupted the co-localization of the beta(1)AR and PSD-95 in cells. Agonist-induced internalization of the beta(1)AR in HEK-293 cells was markedly attenuated by PSD-95 co-expression, whereas co-expression of PSD-95 has no significant effect on either desensitization of the beta(1)AR or beta(1)AR-induced cAMP accumulation. Furthermore, PSD-95 facilitated the formation of a complex between the beta(1)AR and N-methyl-d-aspartate receptors, as assessed by co-immunoprecipitation. These data reveal that PSD-95 is a specific beta(1)AR binding partner that modulates beta(1)AR function and facilitates physical association of the beta(1)AR with synaptic proteins, such as the N-methyl-d-aspartate receptors, which are known to be regulated by beta(1)AR stimulation. | lld:pubmed |
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| pubmed-article:10995758 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10995758 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10995758 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10995758 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:10995758 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10995758 | pubmed:author | pubmed-author:LefkowitzR... | lld:pubmed |
| pubmed-article:10995758 | pubmed:author | pubmed-author:HallR ARA | lld:pubmed |
| pubmed-article:10995758 | pubmed:author | pubmed-author:LazA LAL | lld:pubmed |
| pubmed-article:10995758 | pubmed:author | pubmed-author:MillerW EWE | lld:pubmed |
| pubmed-article:10995758 | pubmed:author | pubmed-author:ConzPP | lld:pubmed |
| pubmed-article:10995758 | pubmed:author | pubmed-author:TangYY | lld:pubmed |
| pubmed-article:10995758 | pubmed:author | pubmed-author:HuL ALA | lld:pubmed |
| pubmed-article:10995758 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10995758 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:10995758 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10995758 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10995758 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10995758 | pubmed:pagination | 38659-66 | lld:pubmed |
| pubmed-article:10995758 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10995758 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10995758 | pubmed:articleTitle | beta 1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of beta 1-adrenergic receptor interaction with N-methyl-D-aspartate receptors. | lld:pubmed |
| pubmed-article:10995758 | pubmed:affiliation | Howard Hughes Medical Institute, Departments of Medicine and Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA. | lld:pubmed |
| pubmed-article:10995758 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10995758 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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