Nuclear export of ribosomal subunits

被引：118

作者：

Johnson, AW ^{[1
]}

Lund, E

Dahlberg, J

机构：

[1] Univ Texas, Sect Mol Genet & Microbiol, Austin, TX 78712 USA

[2] Univ Texas, Inst Mol & Cellular Biol, Austin, TX 78712 USA

[3] Univ Wisconsin, Dept Biomol Chem, Madison, WI 53706 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2002年 / 27卷 / 11期

关键词：

D O I：

10.1016/S0968-0004(02)02208-9

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：

The partitioning of cells by a nuclear envelope ensures that precursors of ribosomes do not interact prematurely with other components of the translation machinery. Ribosomal subunits are assembled in nucleoli and exported to the cytoplasm in a CRM1/Ran-GTP-dependent fashion. Export of the large (60S) subunit requires a shuttling adaptor protein, NMD3, which binds to mature, correctly folded subunits. Immature or defective particles do not bind NMD3 and thus are excluded from the export pathway. This structural proofreading is extended into the cytoplasm, where it is believed that several energy-requiring steps release shuttling factors from the subunit, allowing it to function in translation.

引用

页码：580 / 585

页数：6

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