Decision Letter: The Molecular Basis for ANE Syndrome Revealed by the Large Ribosomal Subunit Processome Interactome
April 2016
TLDR ANE syndrome is caused by a mutation in the RBM28 protein that disrupts ribosome assembly.
The study explored the molecular basis of ANE syndrome, a ribosomopathy linked to a mutation in the RBM28 protein, using yeast as a model. The mutation, a leucine to proline substitution, impaired the function of Nop4, the yeast equivalent of RBM28, disrupting its role in ribosome assembly and leading to growth defects and faulty pre-rRNA processing. The mutation altered RBM28 protein folding, affecting its interactions with other proteins. The research concluded that these disruptions were central to ANE syndrome's pathogenesis, observed in a study of 5 boys from the same family. The study also found that the RNA recognition motifs 3 and 4 of Nop4 were crucial for its interactions and function, as they could compensate for growth defects in yeast lacking endogenous Nop4.
