Jones Teresa L Z
Division of Diabetes, Endocrinology and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Methods Enzymol. 2004;389:33-55. doi: 10.1016/S0076-6879(04)89003-7.
Palmitoylation, the reversible, post-translational addition of palmitate to cysteine residues, occurs on several regulators of G-protein signaling (RGS) proteins. Palmitoylation can occur near the amino terminus, as for RGS4 and RGS16, but can also occur on a cysteine residue in the alpha4 helix of the RGS box, which is conserved in most RGS proteins. For some of the RGS proteins, palmitoylation is required to turn off G-protein signaling by accelerating GTP hydrolysis on the Galpha subunit. This article discusses the role of palmitoylation in RGS function and protocols are given for metabolic and in vitro labeling of RGS proteins with [3H]palmitate and measurement of GTP hydrolysis in membranes.
棕榈酰化是指在翻译后将棕榈酸可逆地添加到半胱氨酸残基上,这种修饰发生在几种G蛋白信号调节(RGS)蛋白上。棕榈酰化可以发生在氨基末端附近,如RGS4和RGS16,也可以发生在RGS结构域α4螺旋中的一个半胱氨酸残基上,大多数RGS蛋白中该残基是保守的。对于一些RGS蛋白来说,棕榈酰化是通过加速Gα亚基上的GTP水解来关闭G蛋白信号所必需的。本文讨论了棕榈酰化在RGS功能中的作用,并给出了用[3H]棕榈酸对RGS蛋白进行代谢和体外标记以及测量膜中GTP水解的实验方案。