Author Response: The Molecular Basis for ANE Syndrome Revealed by the Large Ribosomal Subunit Processome Interactome
April 2016
TLDR Defective protein folding due to a mutation is key in ANE syndrome.
The study explored the molecular basis of ANE syndrome by examining a missense mutation in the nucleolar protein RBM28, using yeast as a model. The mutation, a leucine to proline substitution, impaired rRNA processing and disrupted protein-protein interactions, particularly affecting the RRM3 domain's structural integrity. The research demonstrated that the RRM3 and RRM4 domains were crucial for Nop4's function through protein interactions, while RRM1 and RRM2 were not. The study provided the first biochemical analysis of this mutation, revealing its impact on ribosome biogenesis and highlighting the critical role of RRMs in protein interactions. Despite some methodological criticisms, the findings offered new insights into ANE syndrome and ribosome synthesis.
