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- W3166675529 abstract "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), undergo phase separation; however, aberrant phase separation is linked to fatal neurodegenerative diseases. Multiple weak interactions between karyopherin-βs and phase separation-prone proteins, such as FG repeats-containing nucleoporins or IDR-containing karyopherin-β cargos, are likely to be important for passing through the nuclear pore complex and maintaining the soluble state of cargo, respectively. In this review, we discuss how karyopherin-βs regulate phase separation to function." @default.
- W3166675529 created "2021-06-22" @default.
- W3166675529 creator A5023084336 @default.
- W3166675529 creator A5067070492 @default.
- W3166675529 date "2021-06-12" @default.
- W3166675529 modified "2023-10-11" @default.
- W3166675529 title "Karyopherin-βs play a key role as a phase separation regulator" @default.
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- W3166675529 doi "https://doi.org/10.1093/jb/mvab072" @default.
- W3166675529 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8457648" @default.
- W3166675529 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34223614" @default.
- W3166675529 hasPublicationYear "2021" @default.
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