Linked Life Data

7776964

Source:http://linkedlifedata.com/resource/pubmed/id/7776964

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-7-10
pubmed:abstractText
Most members of the family of G protein-coupled receptors have one or more conserved cysteine residues in their carboxy-terminal cytoplasmic tails which are believed to be consensus sites for palmitoylation. Indeed, a growing number of G protein-coupled receptors (rhodopsin, beta 2-, and alpha 2-adrenergic receptors) have now been shown to have palmitic acid covalently attached to this position. In the case of the beta 2-adrenergic receptor, it was also reported that mutation of the palmitoylated cysteine to glycine greatly diminished the ability of this receptor to interact with and activate Gs. Mutation of this conserved cysteine appears to have little or no effect on the ability of other members of this receptor family (rhodopsin, alpha 2-adrenergic and M2 muscarinic) to activate their cognate G proteins, however. The studies presented here were designed to determine whether another Gs-coupled receptor, the LH/CG receptor, is palmitoylated, and whether this modification is important for receptor function. To facilitate biochemical analysis, we examined these issues using cell lines stably transfected with the wild type LH/CG receptor (LHR-wt) or with a mutant receptor in which the two conserved cysteins were mutated to alanines (designated LHR-C621,622A). Our results show that LHR-wt is palmitoylated but that LHR-C621,622A is not. We also show that LHR-C621,622A is capable of binding human CG (hCG) and transducing the cAMP signal. The main difference that we detected between the wild type and mutant receptor is that the latter is trapped intracellularly and does not appear to mature into the 85 kilodalton protein previously identified as the mature cell surface LH/CG receptor.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0888-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
141-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The lutropin/choriogonadotropin receptor is palmitoylated at intracellular cysteine residues.
pubmed:affiliation
Department of Pharmacology, University of Iowa College of Medicine, Iowa City 52242-1109, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't