{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Koning HJ"],"funding":["Tracey Banivanua Mar Fellowship","Clifford Bradley Robertson and Gwendoline Florence Anne Robertson Research Endowment Fund","National Health and Medical Research Council","Motor Neurone Disease Research Australia","Australian Research Council"],"pagination":["gkae1198"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11754644"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["53(2)"],"pubmed_abstract":["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 implicat"],"journal":["Nucleic acids research"],"pubmed_title":["Structural plasticity of the coiled-coil interactions in human SFPQ."],"pmcid":["PMC11754644"],"funding_grant_id":["FT180100204","DP160102435","APP1147496","LE120100092","DP220103667","LE140100096"],"pubmed_authors":["Knott GJ","Monahan G","Ryan TM","Lee M","Marshall AC","Koning HJ","Lai JY","Pullakhandam A","Whitten A","Bond CS","Stroeher E","Fox AH"],"additional_accession":[]},"is_claimable":false,"name":"Structural plasticity of the coiled-coil interactions in human SFPQ.","description":"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 implicat","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-04-15T03:27:30.016Z","creation":"2025-04-05T00:26:11.532Z"},"accession":"S-EPMC11754644","cross_references":{"pubmed":["39698821"],"doi":["10.1093/nar/gkae1198"]}}