Unique motif for nucleolar retention and nuclear export regulated by phosphorylation

被引:33
作者
Catez, F
Erard, M
Schaerer-Uthurralt, N
Kindbeiter, K
Madjar, JJ
Diaz, JJ
机构
[1] Fac Med Lyon RTH Laennec, INSERM, U369, F-69372 Lyon 08, France
[2] Inst Pharmacol & Biol Struct, F-31077 Toulouse 4, France
关键词
D O I
10.1128/MCB.22.4.1126-1139.2002
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1126 / 1139
页数:14
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