biostudies-literatureKoning HJTracey Banivanua Mar FellowshipClifford Bradley Robertson and Gwendoline Florence Anne Robertson Research Endowment FundNational Health and Medical Research CouncilMotor Neurone Disease Research AustraliaAustralian Research Councilgkae1198https://www.ebi.ac.uk/biostudies/studies/S-EPMC11754644biostudies-literatureUnknown53(2)The proteins SFPQ (splicing Factor Proline/Glutamine rich) and NONO (non-POU domain-containing octamer-binding protein) are mammalian members of the Drosophila Behaviour/Human Splicing (DBHS) protein family, which share 76% sequence identity in their conserved 320 amino acid DBHS domain. SFPQ and NONO are involved in all steps of post-transcriptional regulation and are primarily located in mammalian paraspeckles: liquid phase-separated, ribonucleoprotein sub-nuclear bodies templated by NEAT1 long non-coding RNA. A combination of structured and low-complexity regions provide polyvalent interaction interfaces that facilitate homo- and heterodimerisation, polymerisation, interactions with oligonucleotides, mRNA, long non-coding RNA, and liquid phase-separation, all of which have been implicatNucleic acids researchStructural plasticity of the coiled-coil interactions in human SFPQ.PMC11754644FT180100204DP160102435APP1147496LE120100092DP220103667LE140100096Knott GJMonahan GRyan TMLee MMarshall ACKoning HJLai JYPullakhandam AWhitten ABond CSStroeher EFox AHfalseStructural plasticity of the coiled-coil interactions in human SFPQ.The proteins SFPQ (splicing Factor Proline/Glutamine rich) and NONO (non-POU domain-containing octamer-binding protein) are mammalian members of the Drosophila Behaviour/Human Splicing (DBHS) protein family, which share 76% sequence identity in their conserved 320 amino acid DBHS domain. SFPQ and NONO are involved in all steps of post-transcriptional regulation and are primarily located in mammalian paraspeckles: liquid phase-separated, ribonucleoprotein sub-nuclear bodies templated by NEAT1 long non-coding RNA. A combination of structured and low-complexity regions provide polyvalent interaction interfaces that facilitate homo- and heterodimerisation, polymerisation, interactions with oligonucleotides, mRNA, long non-coding RNA, and liquid phase-separation, all of which have been implicat2025-01-01T00:00:00Z2025 Jan2026-04-15T03:27:30.016Z2025-04-05T00:26:11.532ZS-EPMC117546443969882110.1093/nar/gkae1198