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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

Structures of the Karyopherins Kap121p and Kap60p Bound to the Nuclear Pore-Targeting Domain of the SUMO Protease Ulp1p

http://hdl.handle.net/2237/26287
http://hdl.handle.net/2237/26287
8fde53a4-7467-43a1-adc8-c48083ea1eca
名前 / ファイル ライセンス アクション
hirano2017JMB.pdf hirano2017JMB.pdf ファイル公開:2018/01/20 (7.6 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2017-05-11
タイトル
タイトル Structures of the Karyopherins Kap121p and Kap60p Bound to the Nuclear Pore-Targeting Domain of the SUMO Protease Ulp1p
言語 en
著者 Hirano, Hidemi

× Hirano, Hidemi

WEKO 71464

en Hirano, Hidemi

Search repository
Kobayashi, Junya

× Kobayashi, Junya

WEKO 71465

en Kobayashi, Junya

Search repository
Matsuura, Yoshiyuki

× Matsuura, Yoshiyuki

WEKO 71466

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 © 2017. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
抄録
内容記述 The budding yeast small ubiquitin-like modifier (SUMO) protease Ulp1p catalyzes both the processing of newly synthesized SUMO to its mature form and the deconjugation of SUMO from target proteins, thereby regulating a wide range of cellular processes including cell division, DNA repair, DNA replication, transcription, and mRNA quality control. Ulp1p is localized primarily at the nuclear pore complex (NPC) through interactions involving the karyopherins Kap121p and Kap95p–Kap60p heterodimer and a subset of nuclear pore-associated proteins. The sequestration of Ulp1p at the nuclear periphery is crucial for the proper control of protein desumoylation. To gain insights into the role of the karyopherins in regulating the localization of Ulp1p, we have determined the crystal structures of Kap121p and Kap60p bound to the N-terminal non-catalytic domain of Ulp1p that is necessary and sufficient for NPC targeting. Contrary to a previous proposal that Ulp1p is tethered to the transport channel of the NPC through unconventional interactions with the karyopherins, our structures reveal that Ulp1p has canonical nuclear localization signals (NLSs): (1) an isoleucine-lysine-NLS (residues 51–55) that binds to the NLS-binding site of Kap121p, and (2) a classical bipartite NLS (residues 154–172) that binds to the major and minor NLS-binding sites of Kap60p. Ulp1p also binds Kap95p directly, and the Ulp1p–Kap95p binding is enhanced by the importin-β-binding domain of Kap60p. GTP-bound Gsp1p (the yeast Ran ortholog) and the exportin Cse1p cooperate to release Ulp1p from the karyopherins, indicating that the stable sequestration of Ulp1p to the NPC would require a karyopherin-independent mechanism to anchor Ulp1p at the NPC.
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.2016.11.029
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 429, 号 2, p. 249-260, 発行日 2017-01-20
著者版フラグ
値 author
URI
識別子 https://doi.org/10.1016/j.jmb.2016.11.029
識別子タイプ DOI
URI
識別子 http://hdl.handle.net/2237/26287
識別子タイプ HDL
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