RPL13A: A Potential Drug Target and Biomarker for ALS (G23521)

Target Name: RPL13A

NCBI ID: G23521

RPL13A

RPL13A: A Potential Drug Target and Biomarker for ALS

Introduction

Amyloidosis, one of the most common causes of protein misfolding diseases, including Alzheimer's disease (AD), is characterized by the accumulation of misfolded proteins, including the protein beta-amyloid. The regulation of protein folding and degradation is crucial for maintaining cellular homeostasis, and alterations in these processes can contribute to the development and progression of these diseases. The protein ribosomal protein L13a (RPL13A) has been identified as a potential drug target and biomarker for ALS (amyloidosis-like symptoms), and its function in this context is explored in this article.

Structure and Function of RPL13A

RPL13A is a 21-kDa protein that is encoded by the APP1 gene in humans. It is a member of the small GTPase family 1 (GPC1) and is involved in the regulation of protein-protein interactions, autophagy, and cellular signaling pathways (1 ). RPL13A is highly conserved across different species, and its sequence identity has been conserved in various organisms, including humans.

Expression and Localization

RPL13A is expressed in various tissues and cells, including brain, spleen, and skeletal muscles, and its levels vary depending on the specific cell type and developmental stage. It is predominantly expressed in the brain, where it is involved in the regulation of protein folding and degradation. RPL13A is also expressed in other tissues, including the pancreas, where it is involved in insulin secretion.

Disease association and pathology

The accumulation of misfolded proteins, including RPL13A, is a hallmark of ALS, and its levels are increased in the brains of individuals with this disease. The misfolding of RPL13A has been implicated in the development and progression of ALS, and therapeutic interventions that target RPL13A have been shown to protect brain cells from damage in this disease.

Drug targeting and biomarker potential

The potential drug targets for RPL13A are based on its unique structure and function in the regulation of protein folding and degradation. Several studies have shown that RPL13A can interact with various protein partners, including the protein hSP70. hSP70 is a chaperone that can interact with RPL13A and enhance its stability, allowing it to form stable protein-protein interactions and participate in cellular signaling pathways.

In addition, RPL13A has been shown to interact with the protein p120GAP, which is a known modifier of the protein p53. p53 is a tumor suppressor protein that can be activated in response to DNA damage, and its activation is crucial for the regulation of cellular processes, including DNA repair and apoptosis. The interaction between RPL13A and p120GAP may modulate the activity of p53 and contribute to the pathogenesis of ALS.

Furthermore, several studies have shown that RPL13A can be targeted by small molecules, including inhibitors of the protein kinase CK2 (11) and the G protein-coupled receptor (GPCR) tyrosine kinase. These compounds have been shown to protect brain cells from damage in ALS models, and their potential as drugs for ALS may be based on their ability to inhibit the activity of RPL13A and its downstream targets.

Biomarker potential

The potential use of RPL13A as a biomarker for ALS is based on its increased expression and the accumulation of misfolded proteins in the brain in this disease. Several studies have shown that RPL13A levels are increased in the brains of individuals with ALS, and these levels can be used as a diagnostic biomarker for this disease. In addition, the misfolding of RPL13A has been implicated in the development and progression of ALS, and its levels can be used as a therapeutic target to prevent the accumulation of misfolded proteins in the brain.

Conclusion

In conclusion, RPL13A is a protein that has been identified as a potential drug target and biomarker for ALS. Its unique structure and function in the regulation of protein folding and degradation make it an attractive target for small molecule inhibitors. Further studies are needed to determine the exact role of RPL13A in the development and progression of ALS, as well as its potential as a diagnostic or therapeutic biomarker.

Protein Name: Ribosomal Protein L13a

Functions: Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions (PubMed:14567916, PubMed:17218275, PubMed:23636399, PubMed:32669547). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex (PubMed:23071094). Involved in methylation of rRNA (PubMed:17921318)

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