Kuroda Y, Suzuki N, Kataoka T
Department of Physiology, Kobe University School of Medicine, Japan.
Science. 1993 Jan 29;259(5095):683-6. doi: 10.1126/science.8430318.
Ras proteins undergo a series of posttranslational modifications that are critical for their cellular function. These modifications are necessary to anchor Ras proteins to the membrane. Yeast Ras2 proteins were purified with various degrees of modification and examined for their ability to activate their effector, adenylyl cyclase. The farnesylated intermediate form of Ras2 had more than 100 times higher affinity for adenylyl cyclase than for the unprocessed form. The subsequent palmitoylation reaction had little effect. In contrast, palmitoylation was required for efficient membrane localization of the Ras2 protein. These results indicate the importance of farnesylation in the interaction of Ras2 with its effector.
Ras蛋白经历一系列对其细胞功能至关重要的翻译后修饰。这些修饰对于将Ras蛋白锚定到膜上是必要的。用不同程度修饰的酵母Ras2蛋白进行纯化，并检测其激活效应器腺苷酸环化酶的能力。Ras2的法尼基化中间形式对腺苷酸环化酶的亲和力比对未加工形式高100多倍。随后的棕榈酰化反应影响很小。相比之下，棕榈酰化是Ras2蛋白有效膜定位所必需的。这些结果表明法尼基化在Ras2与其效应器相互作用中的重要性。
