Cross regulation of RNA Binding Proteins and Ordered Protein Aggregation

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Many RNA binding proteins contain a glycine-rich domain (GRD). GRD-containing RBPs are tightly regulated in order to avoid spontaneous self-assembly/aggregation into cytoplasmic inclusions and/or their nuclear depletion. Homotypic (and heterotypic) protein-protein interactions mediated by the GRD may regulate RBP activity, functional specificity, and subcellular localization. hnRNP A1 is a highly abundant GRD-containing RBP. It exists in two main splice forms: A1 and A1B, the latter arising from the inclusion of an alternative exon 7B which effectively expands the C-terminal GRD by 56 residues. While hnRNP A1 is a well-known regulator of constitutive and alternative splicing, little information is available on this longer isoform. A recent paper describes a point mutation of a conserved residue (D262N) located within the GRD of hnRNP A1 that can drive hnRNP A1 aggregation. The functional consequence(s) of hnRNP A1 aggregation is (are) unknown.