Target intelligence / Profile preview

60S acidic ribosomal protein P1 (RPLP1)

Target
RPLP1
Molecular classification
Ribosomal protein, Structural component of ribosome, Other
01

Overview

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].

Other names
Large ribosomal subunit protein P1RRP1LP1P1RPP1Acidic ribosomal phosphoprotein P1Ribosomal protein, large, P1Ribosomal protein lateral stalk subunit P1Ribosomal phosphoprotein P1
02

Mechanism of action

Not a therapeutic drug target, but ricin and some ribosome-inactivating proteins bind to the P-stalk to inactivate ribosomes and block translation[4]

03

Biological functions

Protein synthesis (translation elongation)Regulation of ribosomal activityCell proliferationCytoplasmic translation
04

Disease associations

Other (no strong direct evidence for major disease association; potentially modulates viral susceptibility and linked to rare syndromes, but not a prominent disease gene)
05

Safety considerations

Essential for protein synthesis; inhibition or loss disrupts translation and cell proliferation, suggesting essentiality and broad toxicity concerns for any interventions[2]
06

Interacting drugs

Ricin (binds to the P-stalk; not a therapeutic drug but relevant as a toxin interacting at this site)[4]

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