Linked Life Data

9662451

Source:http://linkedlifedata.com/resource/pubmed/id/9662451

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-7-29
pubmed:abstractText
We have recently reported that G alpha12 is acylated with palmitic acid [Veit et al., FEBS Lett. 339 (1994) 160-164]. Here we identify cysteine 11 as the sole palmitoylation site and assess the function of G alpha12 palmitoylation after expression of wild type and acylation-deficient mutant in insect cells. Our experimental approach yielded the following results. (1) Palmitoylation of G alpha12 has no influence on the subunit interactions. (2) Palmitoylation promotes membrane binding of G alpha12 when this protein is expressed alone. Membrane attachment of the heterotrimer occurs independent of the presence of fatty acids in G alpha12. (3) Assays for agonist-stimulated binding of [35S]GTPgammaS after expression of the human thrombin receptor (PAR1) along with G alpha12 and the betagamma subunits revealed a 70% inhibition with the palmitoyl-deficient mutant.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
429
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
370-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
A cysteine-11 to serine mutant of G alpha12 impairs activation through the thrombin receptor.
pubmed:affiliation
Institut für Immunologie und Molekularbiologie, Freie Universität Berlin, City Campus Veterinary Faculty, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't