Abstract
The ribosome, which is present in all three domains of life, plays a well-established, critical role in the translation process by decoding messenger RNA into protein. Ribosomal proteins, in contrast, appear to play non-translational roles in growth, differentiation, and disease. We recently discovered that ribosomes are involved in reverting cellular potency to a multipotent state. Ribosomal incorporation (the uptake of free ribosome by living cells) can direct the fate of both somatic and cancer cells into multipotency, allowing them to switch cell lineage. During this process, both types of cells experienced cell-cycle arrest and cellular stress while remaining multipotent. This review provides a molecular perspective on current insights into ribosome-induced multipotency and sheds light on how a common stress-associated mechanism may be involved. We also discuss the impact of this phenomenon on cancer cell reprogramming and its potential in cancer therapy.
Highlights
Cellular potency refers to the ability of a cell to differentiate into a different cell type
We recently demonstrated that exogenous ribosomal incorporation into somatic and cancer cells causes the reversal of cell fate into a multipotent state [16,22,23,24]
Ribosome-mediated multipotency introduced a new paradigm in cell reprogramming study
Summary
Cellular potency refers to the ability of a cell to differentiate into a different cell type. The functional role of the ribosome as an in vitro de-differentiating factor is a recent discovery in the field of cell reprogramming; the molecular mechanism underlying ribosome-mediated multipotency is unknown. Cancer cells are less specialized than somatic cells, with uncontrolled proliferation, mutation, and altered epigenetics [25,26] Both somatic and cancer cells undergo cell-cycle arrest, sphere formation, and multipotency when subjected to ribosome incorporation, suggesting that a similar mechanism is at work. Such an effect on the cells has the potential to be therapeutic. During ribosome-mediated reprogramming, exogenous His-tagged ribosomal proteins L12 have been found in the nucleus of the reprogrammed cell and might have a similar functional role interacting with transcription factors. It is unclear whether these ribosomal proteins function as free ribosomal proteins separately from their respective complexes
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