{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yoshizawa T"],"funding":["JSPS KAKENHI","Uehara Memorial Foundation","AMED Practical Research Project for Rare/Intractable Diseases","Ralph and Marian Falk Medical Research Trust, Frick Foundation for ALS Research","National Institute of General Medical Sciences","NIGMS NIH HHS","Dr. Ralph and Marian Falk Medical Research Trust, Frick Foundation for ALS Research"],"pagination":["15-23"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8457648"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["170(1)"],"pubmed_abstract":["Recent studies have revealed that cells utilize liquid-liquid phase separation (LLPS) as a mechanism in assembly of membrane-less organelles, such as RNP granules. The nucleus is a well-known membrane-bound organelle surrounded by the nuclear envelope; the nuclear pore complex on the nuclear envelope likely applies LLPS in the central channel to facilitate selective biological macromolecule exchange. Karyopherin-β family proteins exclusively pass through the central channel with cargos by dissolving the phase separated hydrogel formed by the phenylalanine-glycine (FG) repeats-containing nucleoporins. Karyopherin-βs also exhibit dissolution activity for the phase separation of cargo proteins. Many cargos, including RNA-binding proteins containing intrinsically disordered regions (IDRs), und"],"journal":["Journal of biochemistry"],"pubmed_title":["Karyopherin-βs play a key role as a phase separation regulator."],"pmcid":["PMC8457648"],"funding_grant_id":["21ek0109558h0001","grant R35GM138109","R35 GM138109","19K16060","grant number 21ek0109558h0001","R35GM138109","grant number 19K16060"],"pubmed_authors":["Guo L","Yoshizawa T"],"additional_accession":[]},"is_claimable":false,"name":"Karyopherin-βs play a key role as a phase separation regulator.","description":"Recent studies have revealed that cells utilize liquid-liquid phase separation (LLPS) as a mechanism in assembly of membrane-less organelles, such as RNP granules. The nucleus is a well-known membrane-bound organelle surrounded by the nuclear envelope; the nuclear pore complex on the nuclear envelope likely applies LLPS in the central channel to facilitate selective biological macromolecule exchange. Karyopherin-β family proteins exclusively pass through the central channel with cargos by dissolving the phase separated hydrogel formed by the phenylalanine-glycine (FG) repeats-containing nucleoporins. Karyopherin-βs also exhibit dissolution activity for the phase separation of cargo proteins. Many cargos, including RNA-binding proteins containing intrinsically disordered regions (IDRs), und","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Sep","modification":"2025-04-18T19:41:40.225Z","creation":"2025-04-07T07:29:20.286Z"},"accession":"S-EPMC8457648","cross_references":{"pubmed":["34223614"],"doi":["10.1093/jb/mvab072"]}}