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Abstract
The eukaryotic proteome has to be precisely regulated at multiple levels of gene expression, from transcription, translation, and degradation of RNA and protein to adjust to several cellular conditions. Particularly at the translational level, regulation is controlled by a variety of RNA binding proteins, translation and associated factors, numerous enzymes, and by post-translational modifications (PTM). Ubiquitination, a prominent PTM discovered as the signal for protein degradation, has newly emerged as a modulator of protein synthesis by controlling several processes in translation. Advances in proteomics and cryo-electron microscopy have identified ubiquitin modifications of several ribosomal proteins and provided numerous insights on how this modification affects ribosome structure and function. The variety of pathways and functions of translation controlled by ubiquitin are determined by the various enzymes involved in ubiquitin conjugation and removal, by the ubiquitin chain type used, by the target sites of ubiquitination, and by the physiologic signals triggering its accumulation. Current research is now elucidating multiple ubiquitin-mediated mechanisms of translational control, including ribosome biogenesis, ribosome degradation, ribosome-associated protein quality control (RQC), and redox control of translation by ubiquitin (RTU). This review discusses the central role of ubiquitin in modulating the dynamism of the cellular proteome and explores the molecular aspects responsible for the expanding puzzle of ubiquitin signals and functions in translation.
Highlights
Ribosomes are one of the most abundant molecular machines in a cell and perform an essential role in gene expression
As our understanding of the global role of ubiquitination expands from a degradation signal to a modulator of a vast array of cellular pathways, a deeper review of ribosome ubiquitination gives insight into the multiple roles ubiquitin can play within translation control
We have discussed how ubiquitin participates in changing ribosomal structure, impacting interactions with ribosome binding factors, and signaling to degrade various components of the ribosome. These mechanisms are all vital to global cellular function, as tight regulation of translation is necessary for proper gene expression and effective use of cellular energy
Summary
Ribosomes are one of the most abundant molecular machines in a cell and perform an essential role in gene expression. Recent studies suggest that only partial correlation exists between the transcriptome and proteome, ranging from a 0.4–0.7 correlation coefficient in yeast [8,9,10,11] This range suggests that significant regulation occurs post-transcriptionally, including at the level of translation [12,13,14,15,16]. Translational control does not occur in a universal manner across a single cell, but varies based on ribosomal subpopulations, with functions specific to cellular localization, transcript targeting, and signaling pathways [24,25] These subpopulations are distinguishable by RNA and ribosomal protein composition [26,27], binding factors [28], intracellular localization [29,30], and post-translational modifications (PTM) [31]. We will elaborate on these expanding roles of ubiquitin in translational control and discuss the impact of ribosomal ubiquitination in defining the proteome and maintaining cellular health
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