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Ribosomal L1 domain-containing protein 1 (RSL1D1) is a nucleolar RNA-binding protein that participates in multiple cellular processes, including cell cycle progression, regulation of cellular senescence, rRNA processing, and apoptosis. It contains an N-terminal ribosomal L1 domain and a lysine-rich C-terminal domain. RSL1D1 is highly expressed in proliferating cells and various cancers, and its expression declines during cellular senescence. Functionally, it promotes cell proliferation by negatively regulating PTEN translation, interacts with c-Myc to prevent its ubiquitination, and suppresses autophagy by interacting with RAN, influencing STAT3 nuclear distribution. RSL1D1 also modulates the p53 pathway by stabilizing HDM2 mRNA and recruiting p53 for degradation, leading to reduced p53 levels and enhanced cancer cell survival. RSL1D1's activity is implicated in the progression, invasion, and metastasis of colorectal and other cancers and its high expression is a poor prognostic marker in these contexts.
no therapeutics directly acting via RSL1D1 currently described; functional mechanisms for the protein itself include suppression of PTEN translation, modulation of p53 ubiquitination via HDM2, interaction with c-Myc, suppression of autophagy through RAN/Sirt7 competition
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