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<jats:title>Abstract</jats:title> <jats:p>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.</jats:p>
収録刊行物
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- The journal of biochemistry
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The journal of biochemistry 170 (1), 15-23, 2021-07
Tokyo : Japanese Biochemical Society
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詳細情報 詳細情報について
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- CRID
- 1523106606073200384
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- NII論文ID
- 40022722268
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- NII書誌ID
- AA00694073
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- ISSN
- 0021924X
- 17562651
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- NDL書誌ID
- 031765341
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- Web Site
- http://id.ndl.go.jp/bib/031765341
- https://ndlsearch.ndl.go.jp/books/R000000004-I031765341
- http://academic.oup.com/jb/advance-article-pdf/doi/10.1093/jb/mvab072/38865599/mvab072.pdf
- http://academic.oup.com/jb/article-pdf/170/1/15/40429009/mvab072.pdf
- https://search.jamas.or.jp/link/ui/2022302867
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- 本文言語コード
- en
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- NDL 雑誌分類
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- ZR2(科学技術--生物学--生化学)
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- データソース種別
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- NDL
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