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60S acidic ribosomal protein P1 (RPLP1) is an acidic ribosomal phosphoprotein that forms part of the P-stalk of the cytoplasmic 60S large ribosomal subunit, essential for the elongation step of protein synthesis[1][3]. It interacts with other proteins, notably P0 (uL10) and P2, to form a pentameric stalk complex that recruits and regulates translational GTPases critical for mRNA translation[1][4]. Unlike most ribosomal proteins, RPLP1 is acidic, and its highly conserved C-terminal region is vital for interaction with translation factors and sensitivity to certain ribosome-inactivating toxins (like ricin)[4]. Loss or dysfunction of P1/P2 proteins impairs ribosome activity and cell growth, but RPLP1 is not by itself a common drug target or disease marker[2][3].\n\nAdditional context:\n- RPLP1 is highly conserved and broadly expressed in eukaryotes, localizing to the cytoplasm where ribosomes are active[1][3].\n- It has no well-established role as a therapeutic target (enzyme, receptor, transporter, etc.) but is deeply involved in protein translation, a core housekeeping process.\n- Disruption affects cellular translation rates and may be deleterious for cell survival[2].\n- Some studies have explored its role in viral infection susceptibility and rare disorders, but there is no consensus on it being a classical disease gene[3].
Not a therapeutic drug target, but ricin and some ribosome-inactivating proteins bind to the P-stalk to inactivate ribosomes and block translation[4]
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