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Ring finger protein 7 (RNF7) is a highly conserved zinc finger protein that acts as an essential subunit of cullin-RING E3 ubiquitin ligase complexes (notably CRLs/SCF). RNF7 mediates the ubiquitination and subsequent proteasomal degradation of a wide array of regulatory proteins, including cell cycle inhibitors (such as p21 and p27) and pro-apoptotic factors, influencing key cellular processes like cell cycle progression, apoptosis, and signal transduction. RNF7 also possesses antioxidant functions, being inducible by redox stimuli and helping neutralize reactive oxygen species. Dysregulation and overexpression of RNF7 are linked to tumor progression, therapy resistance, and poor prognosis in several cancers, making it a promising candidate for therapeutic intervention and biomarker development[1][2][3][5][7].
Inhibition or silencing of RNF7 upregulates tumor suppressor proteins (e.g., p21, p27, NOXA), inactivates ERK1/2 and NF-κB pathway, suppresses proliferation and increases chemosensitivity[2][4]. As an E3 ligase, RNF7 catalyzes ubiquitination and proteasomal degradation of numerous substrate proteins, regulating cell fate.
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