{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,7,21]],"date-time":"2024-07-21T21:52:44Z","timestamp":1721598764417},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2003,12,1]]},"abstract":"<jats:p>The \u03b1 and \u03b2\u03b3 subunits of heterotrimeric G-proteins contain specific lipid modifications, which are required for their biological function. However, the relevance of these modifications to the interactions within the heterotrimeric G-protein is not fully understood. In order to explore the role of the S-prenyl moiety of the isoprenylated \u03b2\u03b3 dimer of retinal transducin, \u03b2\u03b3t, in the formation of the heterotrimeric complex with the corresponding N-acylated \u03b1 subunit, \u03b1t, we employed purified fully processed subunits, which are soluble in aqueous solutions without detergents. Pertussis-toxin-mediated [32P]ADP-ribosylation of \u03b1t is strongly stimulated (\u224810-fold) in the presence of \u03b2\u03b3t and can thus serve as a measure for heterotrimer formation. Using this assay, preincubation of \u03b1t with S-prenyl analogues containing farnesyl or geranylgeranyl moieties was found to inhibit heterotrimer formation in a dose-dependent manner. The inhibition was competitive and reversible, as indicated by its reversal upon increase of the \u03b2\u03b3t dimer concentration or by removal of the S-prenyl analogue using gel filtration. The competitive nature of the inhibition is supported by the marked attenuation of the inhibition when the S-prenyl analogue was added to \u03b1t together with or after \u03b2\u03b3t. The inhibition does not involve interaction with the \u03b1t acyl group, since an S-prenyl analogue inhibited the [32P]ADP-ribosylation of an unlipidated \u03b1t mutant. These data suggest the existence of a hitherto unrecognized S-prenyl-binding site in \u03b1t, which is critical for its interaction with prenylated \u03b2\u03b3t.<\/jats:p>","DOI":"10.1042\/bj20030578","type":"journal-article","created":{"date-parts":[[2003,11,24]],"date-time":"2003-11-24T22:02:17Z","timestamp":1069711337000},"page":"449-456","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Studies on G-protein \u03b1\u00b7\u03b2\u03b3 heterotrimer formation reveal a putative S-prenyl-binding site in the \u03b1 subunit"],"prefix":"10.1042","volume":"376","author":[{"given":"Alexander","family":"DIETRICH","sequence":"first","affiliation":[{"name":"Department of Pharmacology and Toxicology, University of Ulm, 89069 Ulm, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexander","family":"SCHEER","sequence":"additional","affiliation":[{"name":"Institute of Pharmacology and Toxicology, University of Lausanne, Lausanne, Switzerland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daria","family":"ILLENBERGER","sequence":"additional","affiliation":[{"name":"Department of Pharmacology and Toxicology, University of Ulm, 89069 Ulm, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoel","family":"KLOOG","sequence":"additional","affiliation":[{"name":"Department of Neurobiochemistry, The George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoav I.","family":"HENIS","sequence":"additional","affiliation":[{"name":"Department of Neurobiochemistry, The George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter","family":"GIERSCHIK","sequence":"additional","affiliation":[{"name":"Department of Pharmacology and Toxicology, University of Ulm, 89069 Ulm, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/376\/2\/449\/712191\/bj3760449.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/376\/2\/449\/712191\/bj3760449.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T12:43:20Z","timestamp":1637585000000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/376\/2\/449\/40913\/Studies-on-G-protein-heterotrimer-formation-reveal"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,12,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2003,12,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20030578","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2003,12,1]]}}}