Linked Life Data

20716856

Source:http://linkedlifedata.com/resource/pubmed/id/20716856

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-9-22
pubmed:abstractText
Among the various dopamine receptors, D(2)-like receptors (D2R, D3R, and D4R) are characterized by a large third cytoplasmic loop, a short carboxyl-terminal tail, and the ability to activate inhibitory G proteins. The diverse activities of D(2)-like receptors are partly mediated by proteins that interact with the third cytoplasmic loop, which regulate receptor signaling, receptor trafficking, and stability. Furthermore, in the case of D2R and D3R genes, mRNA splicing generates isoforms in the region of the third cytoplasmic loop. The gene encoding D2R gives rise to two isoforms, termed the dopamine D(2) receptor long isoform (D2LR) and the dopamine D(2) receptor short isoform (D2SR), which lacks 29 amino acids of the D2LR within the third cytoplasmic loop. The D3R gene also produces at least seven distinct alternative splicing variants including D3nf, in which 98 base pairs in the carboxyl-terminal region of the third intracellular loop are deleted. In this review, we focus on proteins interacting with the dopamine D(2)/D(3) receptors in the third cytoplasmic loop. We also define a novel binding protein, heart-type fatty acid-binding protein (H-FABP), which specifically interacts with the 29 D2LR amino acids deleted in D2SR and document its function in D2LR signaling.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1347-8648
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25-31
pubmed:dateRevised
2011-10-24
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Advanced research on dopamine signaling to develop drugs for the treatment of mental disorders: proteins interacting with the third cytoplasmic loop of dopamine D2 and D3 receptors.
pubmed:affiliation
Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University, Japan.
pubmed:publicationType
Journal Article, Review