| Summary: | Tudor-SN (Tudor staphylococcal nuclease), also known as p100 or SND1 (Staphylococcal nuclease and Tudor domain containing 1), is a structurally conserved protein with diverse functions. Emerging evidence indicates that Tudor-SN plays an essential role in both physiological and pathological processes. Under physiological conditions, Tudor-SN regulates DNA transcription, RNA splicing, RNA stability, RNA interference, and RNA editing, and it is essential for a series of cellular biological events, such as cell cycle progression, cell metabolism, and cell survival, in response to harmful stimuli; thus, Tudor-SN functions as a “friend” to the body. However, Tudor-SN is highly expressed in most tumor cells. As an oncoprotein, Tudor-SN is closely associated with the initiation, development, and metastasis of tumors; thus, Tudor-SN functions as a “foe” to the body. What is the potential mechanism by which Tudor-SN switches from its role as “friend” to its role as “foe”? In this study, we review and summarize the available evidence regarding Tudor-SN protein structure, expression, modification, and mutation to present a novel model of Tudor-SN role switching. This review provides a comprehensive insight into the functional significance of the Tudor-SN protein under physiological and pathological conditions as well as corresponding therapeutic strategies that target Tudor-SN.
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