Ribosomal protein L11 (RPL11)

Ribosomal protein L11 (RPL11) is a component of the large (60S) subunit of eukaryotic ribosomes, where it contributes to the assembly and functional integrity of the ribosome, enabling efficient protein synthesis[1][3][7]. Belonging to the L5P family, RPL11 is essential for the maturation of ribosomal RNA and the large subunit itself[3]. It has additional non-ribosomal roles, notably in mediating stress responses when ribosome biogenesis is perturbed: RPL11 accumulates in the nucleoplasm and inhibits the ubiquitin ligase MDM2, leading to activation and stabilization of the tumor suppressor protein p53, thus linking ribosome assembly to cell cycle arrest and apoptosis[3][5]. Mutations in RPL11 are a recognized cause of Diamond-Blackfan anemia, a congenital disorder affecting blood cell production and frequently associated with specific congenital anomalies[1]. Some drugs, such as the antibiotic thiostrepton, interact with the RPL11 binding site, inhibiting ribosomal function by inducing conformational changes in the protein[2][4]. RPL11’s close relationship with cell growth and the p53 tumor suppressor pathway places it at the intersection of ribosome biogenesis, cell cycle regulation, and disease, especially cancer and ribosomopathies[3][5][7].

Other names

60S ribosomal protein L11large ribosomal subunit protein uL5L11uL5CLL-associated antigen KW-12cell growth-inhibiting protein 34DBA7GIG34

Inhibition of ribosomal function (by thiostrepton), Modulation of p53/TP53 pathway (by perturbing ribosome biogenesis leading to p53 stabilization)