La ribonucleoprotein domain family member 6 (LARP6)

La ribonucleoprotein domain family member 6 (LARP6) is a specialized RNA-binding protein that serves as a master regulator of type I collagen synthesis (UniProt Q9BRS8). It specifically binds to a conserved 5' stem-loop (5' SL) structure found in the mRNAs of collagen alpha 1(I) and alpha 2(I), which is essential for their coordinated translation and the assembly of collagen heterotrimers (Stefanovic et al., 2010, PMID: 20852255). Due to its central role in collagen production, LARP6 is a significant therapeutic target for fibrotic diseases, including liver cirrhosis, pulmonary fibrosis, and scleroderma, where excessive collagen deposition leads to organ failure (Challa & Stefanovic, 2011, PMID: 21454521). Experimental small molecules, such as Compound 6 (C6), have been developed to disrupt the LARP6-mRNA interaction, demonstrating the potential to selectively reduce collagen synthesis without affecting other protein production (Manojlovic & Stefanovic, 2012, PMID: 22431518). Additionally, LARP6 has been linked to cancer progression and metastasis, potentially through its influence on the extracellular matrix and epithelial-mesenchymal transition (Zhang et al., 2020). Targeting LARP6 provides a high degree of specificity for collagen-related pathologies, offering a potential advantage over broader, more toxic anti-fibrotic strategies.

Other names

LARP6ACHNLa-related protein 6La ribonucleoprotein-related domain family member 6

Inhibition of the interaction between the LARP6 protein and the 5' stem-loop (5' SL) structure of collagen alpha 1(I) and alpha 2(I) mRNAs to suppress the coordinated translation of type I collagen.