Faure S, Morin N, Dorée M
Centre de Recherches de Biochimie Macromoléculaire, CNRS, Montpellier, France.
Oncogene. 1998 Sep 10;17(10):1215-21. doi: 10.1038/sj.onc.1202056.
It has been shown previously that protein kinase A (PKA) maintains Xenopus oocytes arrested at G2, at least in part by preventing c-mos translation, but how PKA controls c-mos translation is not known. Using microinjection of recombinant c-mos, which still activates MAP kinase in the presence of active PKA, we have found that PKA does not exert any effect on translation of endogenous c-mos if MAP kinase is first activated. Even though they accumulate c-mos and contain MAP kinase activity as high as control oocytes, oocytes do not exit G2 in the presence of active PKA. These results are discussed in connection with recent findings on regulation of c-raf activity.
先前已经表明，蛋白激酶A（PKA）使非洲爪蟾卵母细胞停滞在G2期，至少部分是通过阻止c-mos的翻译来实现的，但PKA如何控制c-mos的翻译尚不清楚。通过显微注射重组c-mos（其在活性PKA存在的情况下仍能激活丝裂原活化蛋白激酶（MAP激酶）），我们发现如果首先激活MAP激酶，PKA对内源性c-mos的翻译没有任何影响。尽管卵母细胞积累了c-mos并且含有与对照卵母细胞一样高的MAP激酶活性，但在活性PKA存在的情况下，卵母细胞不会退出G2期。结合最近关于c-raf活性调节的研究结果对这些结果进行了讨论。
