由磷酸化调节的核仁保留和核输出的独特基序。
Unique motif for nucleolar retention and nuclear export regulated by phosphorylation.
作者信息
Catez Frédéric, Erard Monique, Schaerer-Uthurralt Nathalie, Kindbeiter Karine, Madjar Jean-Jacques, Diaz Jean-Jacques
机构信息
INSERM U369, Faculté de Médecine Lyon-René Théophile Hyacinthe Laennec, 69372 Lyon Cedex 08, France.
出版信息
Mol Cell Biol. 2002 Feb;22(4):1126-39. doi: 10.1128/MCB.22.4.1126-1139.2002.
Abstract
By microinjecting purified glutathione S-transferase linked to all or parts of herpes simplex virus type 1 US11 protein into either the nucleus or the cytoplasm, we have demonstrated that this nucleolar protein exhibits a new type of localization signal controlling both retention in nucleoli and export to the cytoplasm. Saturated mutagenesis combined with computer modeling allowed us to draw the fine-structure map of this domain, revealing a new proline-rich motif harboring both activities, which are temperature dependent and regulated by phosphorylation. Finally, crossing the nuclear pore complex from the cytoplasm to the nucleus is an energy-dependent process for US11 protein, while getting to nucleoli through the nucleoplasm is energy independent.
摘要
通过将与单纯疱疹病毒1型US11蛋白的全部或部分相连的纯化谷胱甘肽S-转移酶显微注射到细胞核或细胞质中，我们已经证明这种核仁蛋白表现出一种新型的定位信号，该信号控制其在核仁中的保留以及向细胞质的输出。饱和诱变结合计算机建模使我们能够绘制该结构域的精细结构图，揭示了一个富含脯氨酸的新基序，该基序具有两种活性，这两种活性均依赖于温度并受磷酸化调节。最后，US11蛋白从细胞质穿过核孔复合体进入细胞核是一个能量依赖的过程，而通过核质到达核仁则不依赖能量。
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