DMA-tudor interaction modules control the specificity of in vivo condensates

• Published in: Cell Vol. 184; no. 14; pp. 3612 - 3625.e17
• Main Authors: Courchaine, Edward M., Barentine, Andrew E.S., Straube, Korinna, Lee, Dong-Ryoung, Bewersdorf, Joerg, Neugebauer, Karla M.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 08.07.2021
• Subjects: Animals; Arginine - analogs & derivatives; Arginine - metabolism; Biomolecular Condensates - metabolism; biomolecular condensation; Cajal body; Cell Nucleus - metabolism; Coiled Bodies - metabolism; condensates; dimethylarginine; DMA; Drosophila melanogaster - metabolism; HEK293 Cells; HeLa Cells; Humans; Ligands; membraneless organelle; Methylation; Mice; microscopy; MLO; Models, Biological; motor neurons; NIH 3T3 Cells; nuclear gem; organelles; post-translational modification; Protein Binding; Protein Domains; Protein Multimerization; Ribonucleoproteins, Small Nuclear - metabolism; SMN Complex Proteins - chemistry; SMN Complex Proteins - metabolism; tudor domains; MLO; biomolecular condensation; membraneless organelle; dimethylarginine; tudor domains; Cajal body; nuclear gem; DMA; post-translational modification

Biomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the “survival of motor neuron protein” (SMN) is implicated in the formation of three different membraneless organelles (MLOs), we hypothesized that SMN promotes condensation. Unexpectedly, we found that SMN...