Proteasome subunit Rpn13 is a novel ubiquitin receptor

被引:512
作者
Husnjak, Koraljka [1 ,2 ]
Elsasser, Suzanne [3 ]
Zhang, Naixia [4 ]
Chen, Xiang [4 ]
Randles, Leah [4 ]
Shi, Yuan [3 ]
Hofmann, Kay [5 ]
Walters, Kylie J. [4 ]
Finley, Daniel [3 ]
Dikic, Ivan [1 ,2 ,6 ]
机构
[1] Univ Frankfurt, Inst Biochem 2, D-60590 Frankfurt, Germany
[2] Mediterranean Inst Life Sci, Tumor Biol Program, Split 21000, Croatia
[3] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
[4] Univ Minnesota, Dept Biochem Mol Biol & Biophys, Minneapolis, MN 55455 USA
[5] Miltenyi Biotec GmbH, D-50829 Cologne, Germany
[6] Univ Split, Sch Med, Dept Immunol, Split 21000, Croatia
关键词
D O I
10.1038/nature06926
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Proteasomal receptors that recognize ubiquitin chains attached to substrates are key mediators of selective protein degradation in eukaryotes. Here we report the identification of a new ubiquitin receptor, Rpn13/ARM1, a known component of the proteasome. Rpn13 binds ubiquitin through a conserved amino-terminal region termed the pleckstrin-like receptor for ubiquitin (Pru) domain, which binds K48-linked diubiquitin with an affinity of approximately 90 nM. Like proteasomal ubiquitin receptor Rpn10/S5a, Rpn13 also binds ubiquitin-like (UBL) domains of UBL- ubiquitin- associated (UBA) proteins. In yeast, a synthetic phenotype results when specific mutations of the ubiquitin binding sites of Rpn10 and Rpn13 are combined, indicating functional linkage between these ubiquitin receptors. Because Rpn13 is also the proteasomal receptor for Uch37, a deubiquitinating enzyme, our findings suggest a coupling of chain recognition and disassembly at the proteasome.
引用
收藏
页码:481 / 488
页数:8
相关论文
共 36 条
[1]   UBA domains of DNA damage-inducible proteins interact with ubiquitin [J].
Bertolaet, BL ;
Clarke, DJ ;
Wolff, M ;
Watson, MH ;
Henze, M ;
Divita, G ;
Reed, SI .
NATURE STRUCTURAL BIOLOGY, 2001, 8 (05) :417-422
[2]   Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis [J].
Bienko, M ;
Green, CM ;
Crosetto, N ;
Rudolf, F ;
Zapart, G ;
Coull, B ;
Kannouche, P ;
Wider, G ;
Peter, M ;
Lehmann, AR ;
Hofmann, K ;
Dikic, I .
SCIENCE, 2005, 310 (5755) :1821-1824
[3]   Regulation of Pax3 by proteasomal degradation of monoubiquitinated protein in skeletal muscle progenitors [J].
Boutet, Stephane C. ;
Disatnik, Marie-Helene ;
Chan, Lauren S. ;
Iori, Kevin ;
Rando, Thomas A. .
CELL, 2007, 130 (02) :349-362
[4]   Rad23 promotes the targeting of proteolytic substrates to the proteasome [J].
Chen, L ;
Madura, K .
MOLECULAR AND CELLULAR BIOLOGY, 2002, 22 (13) :4902-4913
[5]  
DEVERAUX Q, 1994, J BIOL CHEM, V269, P7059
[6]   Proteasome subunit Rpn1 binds ubiquitin-like protein domains [J].
Elsasser, S ;
Gali, RR ;
Schwickart, M ;
Larsen, CN ;
Leggett, DS ;
Müller, B ;
Feng, MT ;
Tübing, F ;
Dittmar, GAG ;
Finley, D .
NATURE CELL BIOLOGY, 2002, 4 (09) :725-730
[7]   Delivery of ubiquitinated substrates to protein-unfolding machines [J].
Elsasser, S ;
Finley, D .
NATURE CELL BIOLOGY, 2005, 7 (08) :742-U10
[8]   Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome [J].
Elsasser, S ;
Chandler-Militello, D ;
Müller, B ;
Hanna, J ;
Finley, D .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (26) :26817-26822
[9]   Analysis of the human protein interactome and comparison with yeast, worm and fly interaction datasets [J].
Gandhi, TKB ;
Zhong, J ;
Mathivanan, S ;
Karthick, L ;
Chandrika, KN ;
Mohan, SS ;
Sharma, S ;
Pinkert, S ;
Nagaraju, S ;
Periaswamy, B ;
Mishra, G ;
Nandakumar, K ;
Shen, BY ;
Deshpande, N ;
Nayak, R ;
Sarker, M ;
Boeke, JD ;
Parmigiani, G ;
Schultz, J ;
Bader, JS ;
Pandey, A .
NATURE GENETICS, 2006, 38 (03) :285-293
[10]   A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3 [J].
Glickman, MH ;
Rubin, DM ;
Coux, O ;
Wefes, I ;
Pfeifer, G ;
Cjeka, Z ;
Baumeister, W ;
Fried, VA ;
Finley, D .
CELL, 1998, 94 (05) :615-623