Paraspeckles are dynamic, ribonucleoprotein bodies found in eukaryotic cell nuclei.  The formation of paraspeckles depends on the transcription of the long non-coding RNA, NEAT1, which acts as a scaffold for the recruitment of some 40 nuclear proteins ^1 2 .  Paraspeckle associated proteins and the regulation of NEAT1 transcription, have been implicated in a variety of human cancers and disease.  Currently, paraspeckles are thought to be stress-responsive warehouses that exhibit transcriptional control via protein/RNA sequestration.  The dynamic accumulation of such a large variety of protein factors in a single ribonuclear body is a unique aspect of paraspeckles and as such could represent a paradigm shift of how ribonuclear proteins are organised within the nucleus. 

The individual paraspeckle protein components are multi-domain proteins containing a combination of protein-binding, RNA-binding, and low complexity domains ² .   This provokes immediate intrigue into investigating the molecular details of how these proteins interact with each other and RNA.  To characterise the paraspeckle interactome, we have carried out large-scale yeast-2-hybrid screens to define paraspeckle protein interactions. Biophysical techniques such as microscale thermophoresis, isothermal titration calorimetry, co-expression, co-crystallisation and small-angle X-ray scattering are subsequently used to validate and characterise interactions.  These techniques will provide detailed insight into the mechanism of paraspeckle proteins and/or RNA interaction and a structural basis for the functional links between these proteins and for the paraspeckle as a whole.  Through this study we hope to gain insight into the paraspeckle complex formation for possible future therapeutic targets.