Effects of farnesylcysteine analogs on protein carboxyl methylation and signal transduction.
Effects of farnesylcysteine analogs on protein carboxyl methylation and signal transduction.
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DOI：
10.1016/s0021-9258(18)54669-x
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发表时间：
1991-11
期刊：
影响因子：
--
通讯作者：
C. Volker;R. A. Miller;W. McCleary;A. Rao;M. Poenie;J. Backer;J. Stock
中科院分区：
文献类型：
--
作者：
C. Volker;R. A. Miller;W. McCleary;A. Rao;M. Poenie;J. Backer;J. Stock
在真核生物中，一些与信号转导相关的蛋白质在羧基末端的S-法尼基半胱氨酸残基上发生了羧甲基化。其中包括RAS超家族成员和异三聚体G蛋白的伽马亚基。催化羧甲基化反应的酶还甲基化小分子，如N-乙酰-S-反式，反式-法尼基-L-半胱氨酸(AFC)。AFC在体外和体内均能抑制p21ras及其相关蛋白的羧甲基化。饱和浓度的AFC对小鼠腹腔巨噬细胞的趋化反应有80%以上的抑制作用。我们的结果表明，在真核细胞中，羧甲基化可能在受体介导的信号转导过程中发挥作用。
Several proteins associated with signal transduction in eukaryotes are carboxyl methylated at COOH-terminal S-farnesylcysteine residues. These include members of the Ras superfamily and gamma-subunits of heterotrimeric G-proteins. The enzymes that catalyze the carboxyl methylation reaction also methylate small molecules such as N-acetyl-S-trans, trans-farnesyl-L-cysteine (AFC). AFC inhibits carboxyl methylation of p21ras and related proteins both in vitro and in vivo. Saturating concentrations of AFC cause a greater than 80% inhibition of chemotactic responses of mouse peritoneal macrophages. Our results suggest that carboxyl methylation may play a role in the regulation of receptor-mediated signal transduction processes in eukaryotic cells.