Effect of nuclear import receptors on liquid–liquid phase separation
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- Yoshizawa Takuya
- College of Life Sciences, Ritsumeikan University
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- Matsumura Hiroyoshi
- College of Life Sciences, Ritsumeikan University
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Abstract
<p>Low-complexity (LC) sequences, regions that are predominantly made up of limited amino acids, are often observed in eukaryotic nuclear proteins. The role of these LC sequences has remained unclear for decades. Recent studies have shown that LC sequences are important in the formation of membrane-less organelles via liquid–liquid phase separation (LLPS). The RNA binding protein, fused in sarcoma (FUS), is the most widely studied of the proteins that undergo LLPS. It forms droplets, fibers, or hydrogels using its LC sequences. The N-terminal LC sequence of FUS is made up of Ser, Tyr, Gly, and Gln, which form a labile cross-β polymer core while the C-terminal Arg-Gly-Gly repeats accelerate LLPS. Normally, FUS localizes to the nucleus via the nuclear import receptor karyopherin β2 (Kapβ2) with the help of its C-terminal proline-tyrosine nuclear localization signal (PY-NLS). Recent findings revealed that Kapβ2 blocks FUS mediated LLPS, suggesting that Kapβ2 is not only a transport protein but also a chaperone which regulates LLPS during the formation of membrane-less organelles. In this review, we discuss the effects of the nuclear import receptors on LLPS.</p>
Journal
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- Biophysics and Physicobiology
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Biophysics and Physicobiology 17 (0), 25-29, 2020-04-04
The Biophysical Society of Japan
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Details 詳細情報について
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- CRID
- 1390002184892417664
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- NII Article ID
- 130007828794
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- ISSN
- 21894779
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- Text Lang
- en
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- Data Source
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- JaLC
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed