RPL4
RPL4 (Ribosomal Protein L4) is a protein that in humans is encoded by the RPL4 gene. This gene is a part of the ribosome, a complex molecular machine that serves as the site of biological protein synthesis. RPL4 is one of the components of the large ribosomal subunit, playing a critical role in the initiation of protein synthesis, RNA binding, and ensuring the accuracy of translation.
Function[edit | edit source]
RPL4 is integral to the function of the ribosome, participating in the assembly of the ribosome itself and the translation of mRNA into protein. It is involved in the early stages of ribosome assembly and is necessary for the proper folding and structural arrangement of the ribosomal RNA (rRNA). This protein is also implicated in the interaction with various ribosomal proteins and translation factors, facilitating the correct positioning of the mRNA and tRNAs within the ribosome.
Genetic Structure[edit | edit source]
The RPL4 gene is located on the human genome and contains several exons that encode the protein. Mutations in this gene can lead to alterations in ribosome function, which may affect cell growth and division, potentially leading to various diseases.
Clinical Significance[edit | edit source]
Alterations in the expression or function of RPL4 can have significant clinical implications. Given its fundamental role in protein synthesis, changes in RPL4 activity can influence cell growth and proliferation. This has been observed in certain types of cancer, where overexpression or mutations in the RPL4 gene may contribute to tumorigenesis. Additionally, due to its role in ribosomal function, mutations in RPL4 have been associated with ribosomopathies, a group of disorders characterized by defects in ribosome biogenesis and function.
Research[edit | edit source]
Research on RPL4 continues to uncover its roles beyond traditional ribosome function, including its involvement in cellular stress responses, apoptosis, and the regulation of gene expression. Understanding the multifaceted roles of RPL4 can provide insights into its potential as a therapeutic target in diseases associated with ribosomal dysfunction and cancer.
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Contributors: Prab R. Tumpati, MD