Casey P J
Department of Molecular Cancer Biology, Duke University Medical Center, Durham, NC 27710.
Curr Opin Cell Biol. 1994 Apr;6(2):219-25. doi: 10.1016/0955-0674(94)90139-2.
Covalent attachment of lipids is a near-universal mechanism through which eukaryotic cells direct and, in some cases, control membrane localization of G proteins. Studies conducted over the past year have substantially advanced our understanding of both the molecular mechanisms and the functional consequences of these modifications. Of particular note are the processes of palmitoylation of the alpha-subunits of heterotrimeric G proteins, and prenylation of members of the Ras superfamily of monomeric G proteins, where recent findings point to unexpected roles for lipid modifications in signaling through these proteins.
脂质的共价连接是一种几乎普遍存在的机制，真核细胞通过这种机制引导并在某些情况下控制G蛋白的膜定位。过去一年进行的研究极大地推进了我们对这些修饰的分子机制和功能后果的理解。特别值得注意的是异源三聚体G蛋白α亚基的棕榈酰化过程，以及单体G蛋白的Ras超家族成员的异戊二烯化过程，最近的研究结果表明脂质修饰在通过这些蛋白进行信号传导中发挥了意想不到的作用。
