FEBS Letters | |
The α‐subunits of G‐proteins G12 and G13 are palmitoylated, but not amidically myristoylated | |
Spicher, Karsten2  Veit, Michael1  Schultz, Günter2  Ponimaskin, Ewgeni1  Schmidt, Michael F.G.1  Harteneck, Christian2  Nürnberg, Bernd2  | |
[1] Institut für Immunologie und Molekularbiologie, Freie Universität Berlin, Fachbereich Veterinärmedizin, Königin-Luise-Str. 49, 14195 Berlin, Germany;Institut für Pharmakologie, Universitätsklinikum Rudolf Virchow, Freie Universität Berlin, Thielallee 69-73, 14195 Berlin, Germany | |
关键词: Palmitoylation; G-protein; G12; G13; Acylation; Baculovirus expression; | |
DOI : 10.1016/0014-5793(94)80406-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The α-subunits of the G-proteins G12 and G13, were expressed with a baculovirus system in insect cells and analysed for acylation. Both proteins incorporated tritiated palmitic and to a lesser extent also tritiated myristic acid. Radiolabel from both fatty acids was sensitive to treatment with neutral hydroxylamine. This result supports a thioester-type fatty acid bond and argues against amidical N-myristoylation. Fatty acid analysis after labeling with [3H]palmitic acid showed that palmitate represents the predominant fatty acid linked to Gα12 and Gα13. Separation of cells into cytosolic and membranous fractions revealed that palmitoylated α-subunits of G12 were exclusively membrane-bound, whereas [35S]methionine-labeled proteins were detected in soluble and particulate fractions. Inhibition of protein synthesis with cycloheximide did not block palmitoylation of the α-subunits. which indicates that palmitoylation occurs independently of protein synthesis.
【 授权许可】
Unknown
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