Abstract
The ribosome, the site for protein synthesis, is composed of ribosomal RNAs (rRNAs) and ribosomal proteins (RPs). The latter have been shown to have many ribosomal and extraribosomal functions. RPs are implicated in a variety of pathological processes, especially tumorigenesis and cell transformation. In this review, we will focus on the recent advances that shed light on the effects of RPs deregulation in different types of cancer and their roles in regulating the tumor cell fate.
Highlights
Protein synthesis is a highly regulated and coordinated process involving the action of ribosomes and a set of translation factors
Ribosome biogenesis occurs in the nucleolus and requires the action of 80 ribosomal proteins (RPs), 4 ribosomal RNAs, other associated proteins and small nucleolar RNAs [1,2]
RPL9 KD inactivates Id-1/nuclear factor-κB (NFB) signaling pathway in HT29 and HCT116 colon cancer cells when compared with the control by phosphorylating IB, which is known to prevent the translocation of NFB into the nucleus and the activation of genes that promote cell survival
Summary
The ribosome, the site for protein synthesis, is composed of ribosomal RNAs (rRNAs) and ribosomal proteins (RPs). The latter have been shown to have many ribosomal and extraribosomal functions. RPs are implicated in a variety of pathological processes, especially tumorigenesis and cell transformation. We will focus on the recent advances that shed light on the effects of RPs deregulation in different types of cancer and their roles in regulating the tumor cell fate. Accepted Manuscript Online: 07 December 2021 Version of Record published: 17 December 2021
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