Prion-like domains (PLDs) are low complexity sequences found in RNA-binding proteins associated with the neurodegenerative disorder amyotrophic lateral sclerosis. Recently, PLDs have been implicated in mediating gene regulation via liquid-phase transitions that drive RNA/protein granule assembly.  Here we report enrichment of PLDs in proteins associated with paraspeckles, nuclear organelles that form around long non-coding RNA. We mapped the interactome network of paraspeckle proteins, identifying hubs with PLDs.  We show that one protein, RBM14, connects key paraspeckle subcomplexes, and confirm these interactions are mediated via its PLD.  We further show that this domain is required to rescue paraspeckle formation in RBM14-depeleted cells.  Similar to another essential paraspeckle protein, FUS, the RBM14 PLD forms hydrogels with amyloid-like properties.  These results not only suggest a role for PLD-mediated liquid-phase transitions in paraspeckle formation, but also highlight this nuclear body as an excellent model system for understanding the perturbation of such processes in neurodegeneration.