Abstract

Ribosomal proteins are expressed at high levels beyond that required for the typical rate of ribosome-subunit production and accumulate in the nucleolus more quickly than all other nucleolar components. This is balanced by continual degradation of unassembled ribosomal proteins in the nucleoplasm, thereby providing a mechanism for mammalian cells to ensure that ribosomal protein levels are never rate limiting for the efficient assembly of ribosome subunits. The dual time-lapse strategy used in this study, combining proteomics and imaging, provides a powerful approach for the quantitative analysis of the flux of newly synthesized proteins through a cell organelle.

Keywords

NucleolusNucleoplasmRibosomal proteinBiologyRibosomeRibosomal RNACell biologyOrganelleMolecular biologyBiochemistryCytoplasmRNAGene

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Year
2007
Type
article
Volume
17
Issue
9
Pages
749-760
Citations
385
Access
Closed

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Yun Wah Lam, Angus I. Lamond, Matthias Mann et al. (2007). Analysis of Nucleolar Protein Dynamics Reveals the Nuclear Degradation of Ribosomal Proteins. Current Biology , 17 (9) , 749-760. https://doi.org/10.1016/j.cub.2007.03.064

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DOI
10.1016/j.cub.2007.03.064