60S acidic ribosomal protein P0 and P1 (RPLP0/RPLP1)

The 60S acidic ribosomal proteins P0 and P1 are essential components of the eukaryotic ribosome's lateral stalk, a dynamic structure critical for protein biosynthesis [1, 3]. P0 serves as the anchor for the stalk, binding directly to the 28S ribosomal RNA, while P1 (along with P2) forms heterodimers that attach to P0 to complete the pentameric P-complex [5, 12]. This stalk is primarily responsible for the recruitment and activation of GTP-dependent translation elongation factors, such as eEF-1 and eEF-2, which are necessary for the movement of the ribosome along mRNA [8, 13]. In clinical contexts, these proteins are significant autoantigens in Systemic Lupus Erythematosus (SLE), where the presence of anti-ribosomal P antibodies is a highly specific marker for the disease and its neuropsychiatric manifestations [2, 13]. Furthermore, P0 and P1 are frequently overexpressed in various malignancies, including breast, liver, and lung carcinomas, where they contribute to increased translational capacity and tumor progression [1, 9]. They also serve as the critical docking site for ribosome-inactivating toxins like ricin and Shiga toxin, which exploit the P-stalk to access the sarcin-ricin loop and halt cellular protein production [13, 17]. Research into targeting these proteins for cancer therapy is ongoing, though their essential role in global translation presents significant challenges for achieving therapeutic selectivity [9, 15].

Other names

60S acidic ribosomal protein P060S acidic ribosomal protein P1Ribosomal protein lateral stalk subunit P0Ribosomal protein lateral stalk subunit P1Acidic ribosomal phosphoprotein P0Acidic ribosomal phosphoprotein P1RPP0RPP1L10EL12PP-stalk proteins

Toxins like ricin and Shiga toxin bind to the conserved C-terminal domain of the P-stalk proteins to gain access to the sarcin-ricin loop of the 28S rRNA, where they exert N-glycosidase activity to inhibit translation [13, 17].