| アイテムタイプ |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2024-07-25 |
| タイトル |
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タイトル |
Mutations linked to neurological disease enhance self-association of low-complexity protein sequences. |
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言語 |
en |
| 言語 |
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|
言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| 著者 |
Xiaoming Zhou
Lily Sumrow
Kyuto Tashiro
Lillian Sutherland
Daifei Liu
Tian Qin
Masato Kato
Glen Liszczak
Steven L McKnight
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| 抄録 |
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内容記述タイプ |
Abstract |
|
内容記述 |
Protein domains of low sequence complexity do not fold into stable, three-dimensional structures. Nevertheless, proteins with these sequences assist in many aspects of cell organization, including assembly of nuclear and cytoplasmic structures not surrounded by membranes. The dynamic nature of these cellular assemblies is caused by the ability of low-complexity domains (LCDs) to transiently self-associate through labile, cross-β structures. Mechanistic studies useful for the study of LCD self-association have evolved over the past decade in the form of simple assays of phase separation. Here, we have used such assays to demonstrate that the interactions responsible for LCD self-association can be dictated by labile protein structures poised close to equilibrium between the folded and unfolded states. Furthermore, missense mutations causing Charcot-Marie-Tooth disease, frontotemporal dementia, and Alzheimer's disease manifest their pathophysiology in vitro and in cultured cell systems by enhancing the stability of otherwise labile molecular structures formed upon LCD self-association. |
| 書誌情報 |
Science (New York, N.Y.)
巻 377,
号 6601,
p. eabn5582,
発行日 2022-07
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| 出版者 |
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出版者 |
American Association for the Advancement of Science |
| ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
1095-9203 |
| PubMed番号 |
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識別子タイプ |
PMID |
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関連識別子 |
35771920 |
| DOI |
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識別子タイプ |
DOI |
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関連識別子 |
10.1126/science.abn5582 |
