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  1. B100 理学部/理学研究科
  2. B100a 雑誌掲載論文
  3. 学術雑誌

Mechanistic Insights from Structural Analyses of Ran-GTPase-Driven Nuclear Export of Proteins and RNAs

http://hdl.handle.net/2237/25107
http://hdl.handle.net/2237/25107
b9a3ccdc-4919-4b6e-abe1-819f62209931
名前 / ファイル ライセンス アクション
Matsuura2016JMB.pdf Matsuura2016JMB.pdf ファイル公開:2017/05/22 (1.7 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2016-11-25
タイトル
タイトル Mechanistic Insights from Structural Analyses of Ran-GTPase-Driven Nuclear Export of Proteins and RNAs
言語 en
著者 Matsuura, Yoshiyuki

× Matsuura, Yoshiyuki

WEKO 67523

en Matsuura, Yoshiyuki

Search repository
アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利
言語 en
権利情報 © 2016. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
キーワード
主題Scheme Other
主題 exportin
キーワード
主題Scheme Other
主題 Ran
キーワード
主題Scheme Other
主題 nuclear export signal
キーワード
主題Scheme Other
主題 nucleoporin
キーワード
主題Scheme Other
主題 nuclear pore complex
抄録
内容記述 Understanding how macromolecules are rapidly exchanged between the nucleus and the cytoplasm through nuclear pore complexes is a fundamental problem in biology. Exportins are Ran-GTPase-dependent nuclear transport factors that belong to the karyopherin-β family and mediate nuclear export of a plethora of proteins and RNAs, except for bulk mRNA nuclear export. Exportins bind cargo macromolecules in a Ran-GTP-dependent manner in the nucleus, forming exportin-cargo-Ran-GTP complexes (nuclear export complexes). Transient weak interactions between exportins and nucleoporins containing characteristic FG (phenylalanine-glycine) repeat motifs facilitate nuclear pore complex passage of nuclear export complexes. In the cytoplasm, nuclear export complexes are disassembled, thereby releasing the cargo. GTP hydrolysis by Ran promoted in the cytoplasm makes the disassembly reaction virtually irreversible and provides thermodynamic driving force for the overall export reaction. In the past decade, X-ray crystallography of some of the exportins in various functional states coupled with functional analyses, single-particle electron microscopy, molecular dynamics simulations, and small-angle solution X-ray scattering has provided rich insights into the mechanism of cargo binding and release and also begins to elucidate how exportins interact with the FG repeat motifs. The knowledge gained from structural analyses of nuclear export is being translated into development of clinically useful inhibitors of nuclear export to treat human diseases such as cancer and influenza.
言語 en
内容記述タイプ Abstract
出版者
言語 en
出版者 Elsevier
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/j.jmb.2015.09.025
ISSN
収録物識別子タイプ PISSN
収録物識別子 0022-2836
書誌情報 en : Journal of Molecular Biology

巻 428, 号 10A, p. 2025-2039, 発行日 2016-05-22
著者版フラグ
値 author
URI
識別子 http://doi.org/10.1016/j.jmb.2015.09.025
識別子タイプ DOI
URI
識別子 http://hdl.handle.net/2237/25107
識別子タイプ HDL
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