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Zinc finger protein ZPR1 is a highly conserved, non-classical zinc finger protein essential for cell viability in eukaryotes. ZPR1 is cytoplasmic in quiescent cells but translocates to the nucleus and accumulates in the nucleolus upon mitogenic stimulation[1]. It is required for normal nucleolar function, especially for pre-rRNA expression and processing—critical steps in ribosome biogenesis[1]. ZPR1 binds the cytoplasmic domain of receptor tyrosine kinases such as the EGFR in its inactive state via its zinc finger motifs[1][3]. Biochemically, ZPR1 has been shown to be an essential bespoke chaperone for eukaryotic translation elongation factor 1A (eEF1A), preventing its misfolding and thereby maintaining proteostasis[2]. ZPR1 is required for cell proliferation; its disruption leads to loss of rRNA, impaired protein synthesis, proteotoxic stress, and cell death[1][2]. No approved drugs are known to selectively target ZPR1, and it is not described as a therapeutic target, but its essential cell viability functions are well established.
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