Tudor-dimethylarginine interactions: the condensed version

Biomolecular condensates (BMCs) can facilitate or inhibit diverse cellular func-tions. BMC formation is driven by noncovalent protein-protein, protein-RNA, and RNA-RNA interactions. Here, we focus on Tudor domain-containing proteins - such as survival motor neuron protein (SMN) - that contribute to BMC formation by binding to dimethylarginine (DMA) modifications on protein ligands. SMN is present in RNA-rich BMCs, and its absence causes spinal mus-cular atrophy (SMA). SMN's Tudor domain forms cytoplasmic and nuclear BMCs, but its DMA ligands are largely unknown, highlighting open questions about the function of SMN. Moreover, DMA modification can alter intramolecular interac-tions and affect protein localization. Despite these emerging functions, the lack of direct methods of DMA detection remains an obstacle to understanding Tudor-DMA interactions in cells.

Automated summary

Biomolecular condensates (BMCs) play a role in cellular functions through protein-protein, protein-RNA, and RNA-RNA interactions. Tudor domain-containing proteins, like SMN, contribute to BMC formation by binding to DMA modifications on protein ligands. SMN's absence causes SMA, and the identity of its DMA ligands is largely unknown, posing questions about its function. DMA modification can also affect protein interactions and localization. However, the lack of direct DMA detection methods hinders the understanding of Tudor-DMA interactions in cells.