POLYLYSINE DOMAIN OF K-RAS 4B PROTEIN IS CRUCIAL FOR MALIGNANT TRANSFORMATION
POLYLYSINE DOMAIN OF K-RAS 4B PROTEIN IS CRUCIAL FOR MALIGNANT TRANSFORMATION
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DOI：
10.1073/pnas.91.26.12730
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发表时间：
1994-12-20
影响因子：
11.1
通讯作者：
COCHRANE, CG
中科院分区：
文献类型：
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作者：
JACKSON, JH;LI, JW;COCHRANE, CG
先前的研究表明，致癌的K-ras4B蛋白膜结合和转化活性都需要翻译后修饰。此外，Hancock et al.汉考克，J.F.，伊利诺伊州帕特森和Matt，C.J.(1990)Cell 63,133-139]发现K-ras 4B的C末端的聚赖氨酸结构域对II-ras 4B膜的结合也是绝对必要的，但令人惊讶的是，转化活性既不需要多赖氨酸结构域，也不需要膜结合。我们曾进行过类似的研究，但我们的结果明显不同，我们的研究表明，多赖氨酸结构域对II-ras 4B的转化活性至关重要。此外，我们还证明，尽管多聚赖氨酸结构域增加了K-ras4B膜的结合，但在没有这个结构域的情况下，可以发生大量的膜结合。最后，虽然我们的研究与K-ras 4B转化活性需要膜结合的观点是一致的，但我们发现膜结合本身并不足以产生有效的K-ras 4B转化活性。
Previous studies have shown that posttranslational modifications are required for both oncogenic K-ras 4B protein membrane binding and transforming activity. In addition, Hancock et al. [Hancock, J. F., Patterson, Il. and Marshall, C. J. (1990) Cell 63, 133-139] found that a polylysine domain contained at the C terminus of K-ras 4B was also absolutely essential for Ii-ras 4B membrane binding but, surprisingly, neither the polylysine domain nor membrane binding was required for transforming activity. We have performed similar studies, but our results are distinctly different, Our studies indicate that the polylysine domain is crucial for Ii-ras 4B transforming activity. Moreover, we demonstrate that although the polylysine domain increases K-ras 4B membrane binding, significant amounts of membrane binding can occur in the absence of this domain. Finally, while our studies are consistent with the notion that membrane binding is required for K-ras 4B transforming activity, we show that membrane binding, in and of itself, is not sufficient for efficient K-ras 4B transforming activity.