<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Yoshizawa T</submitter><funding>JSPS KAKENHI</funding><funding>Uehara Memorial Foundation</funding><funding>AMED Practical Research Project for Rare/Intractable Diseases</funding><funding>Ralph and Marian Falk Medical Research Trust, Frick Foundation for ALS Research</funding><funding>National Institute of General Medical Sciences</funding><funding>NIGMS NIH HHS</funding><funding>Dr. Ralph and Marian Falk Medical Research Trust, Frick Foundation for ALS Research</funding><pagination>15-23</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8457648</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>170(1)</volume><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</pubmed_abstract><journal>Journal of biochemistry</journal><pubmed_title>Karyopherin-βs play a key role as a phase separation regulator.</pubmed_title><pmcid>PMC8457648</pmcid><funding_grant_id>21ek0109558h0001</funding_grant_id><funding_grant_id>grant R35GM138109</funding_grant_id><funding_grant_id>R35 GM138109</funding_grant_id><funding_grant_id>19K16060</funding_grant_id><funding_grant_id>grant number 21ek0109558h0001</funding_grant_id><funding_grant_id>R35GM138109</funding_grant_id><funding_grant_id>grant number 19K16060</funding_grant_id><pubmed_authors>Guo L</pubmed_authors><pubmed_authors>Yoshizawa T</pubmed_authors></additional><is_claimable>false</is_claimable><name>Karyopherin-βs play a key role as a phase separation regulator.</name><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</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Sep</publication><modification>2025-04-18T19:41:40.225Z</modification><creation>2025-04-07T07:29:20.286Z</creation></dates><accession>S-EPMC8457648</accession><cross_references><pubmed>34223614</pubmed><doi>10.1093/jb/mvab072</doi></cross_references></HashMap>