Ribosomal Protein L38 Activators

Part of the mTOR pathway, rapamycin, can decrease ribosomal protein synthesis, which may lead to compensatory mechanisms that affect the incorporation of RPL38 into the ribosome. Puromycin and cycloheximide are classic protein synthesis inhibitors that cause premature chain termination and inhibit translational elongation, respectively. Their actions result in changes in ribosomal stability and could lead to altered feedback regulation affecting RPL38. Similarly, chloramphenicol and erythromycin, though primarily targeting bacterial ribosomes, are useful tools in studying ribosomal function and can indirectly inform on the dynamics of eukaryotic ribosomes, including RPL38's role.

Tunicamycin, by inducing ER stress, can influence the rate of ribosomal protein production, while homoharringtonine and anisomycin, by targeting the elongation phase of protein synthesis, can affect ribosomal dynamics and potentially the activity of RPL38. Ricin, a potenttoxin that inactivates the ribosome, causes cellular stress responses that may include changes in the production or assembly of ribosomal proteins like RPL38. Some chemicals do not directly activate RPL38 but influence ribosome function and protein synthesis. These chemicals can cause cells to alter ribosome assembly and function, which can indirectly affect RPL38. Sparsomycin and emetine interfere with peptide bond formation and protein synthesis, potentially leading to changes in the ribosomal protein complement to compensate for inhibited function. Pactamycin, by inhibiting translational initiation, may also trigger cellular responses that impact ribosome assembly, indirectly influencing RPL38 activity.