Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-3-5
pubmed:abstractText
Regulators of G-protein signalling (RGS) are a family of proteins that interact with G-proteins to regulate negatively G-protein coupled receptor (GPCR) signalling. In addition to a conserved core domain that is necessary and sufficient for their GTPase activating protein (GAP) like activity, RGSs possess N- and C-terminal motifs that confer distinct functional differences. In order to identify the role of the non-RGS region of human RGS1, we have characterized a series of fusions between RGS1 and GFP in a yeast mutant lacking the RGS containing SST2 gene. Using both halo assays as well as a GPCR responsive FUS1-LacZ reporter gene, we demonstrate that a RGS1-GFP fusion inhibits GPCR signalling in yeast while GFP fusions containing either the N-terminus non RGS sequence of RGS1(1-68) or the sequence containing the RGS box of RGS1(68-197) produce proteins that retain RGS1 activity. These results suggest that both the N-terminal and the RGS box of RGS1 function to inhibit signalling. Analysis of a series of mutants spanning the entire N-terminal non-RGS region of RGS1 produced by conservative segment exchange (CSE) mutagenesis showed little loss of function in yeast. This suggests that the overall structure of the N-terminal region of RGS1 rather than specific motifs or residues is required for its function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0898-6568
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
413-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
The N-terminal non-RGS domain of human regulator of G-protein signalling 1 contributes to its ability to inhibit pheromone receptor signalling in yeast.
pubmed:affiliation
Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't