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

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• 作者：Hidemi Hirano¹ ; ² ; Junya Kobayashi¹ ; Yoshiyuki Matsuura¹ ; ² ; ^{matsuura.yoshiyuki@d.mbox.nagoya-u.ac.jp}
• 关键词：SUMO ; small ubiquitin-like modifier ; Ulp ; ubiquitin-like protein-specific protease ; SENP ; sentrin-specific protease ; NPC ; nuclear pore complex ; NLS ; nuclear localization signal ; cNLS ; classical NLS ; GST ; glutathione S-transferase ; IBB ; importin-β-binding ; AEBSF ; 4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride ; PEG ; polyethylene glycol ; PDB ; Protein Data Bank
• 刊名：Journal of Molecular Biology
• 出版年：2017
• 出版时间：20 January 2017
• 年：2017
• 卷：429
• 期：2
• 页码：249-260
• 全文大小：1669 K
• 卷排序：429

文摘

The NPC-associated SUMO protease Ulp1p regulates numerous cellular processes. The karyopherins bind the non-catalytic domain of Ulp1p and target Ulp1p to the NPC. Structures of the Kap121p–Ulp1p complex and the Kap60p–Ulp1p complex are reported. The non-catalytic domain of Ulp1p contains canonical NLSs. GTP-bound Gsp1p and Cse1p cooperate to release Ulp1p from the karyopherins.