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Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome.

Verma R, Aravind L, Oania R, McDonald WH, Yates JR 3rd, Koonin EV, Deshaies RJ.

Science. 2002 Oct 18;298(5593):611-5. Epub 2002 Aug 15.


Molecular biology. New proteases in a ubiquitin stew.

Hochstrasser M.

Science. 2002 Oct 18;298(5593):549-52. No abstract available.


Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1.

Cope GA, Suh GS, Aravind L, Schwarz SE, Zipursky SL, Koonin EV, Deshaies RJ.

Science. 2002 Oct 18;298(5593):608-11. Epub 2002 Aug 15.


A cryptic protease couples deubiquitination and degradation by the proteasome.

Yao T, Cohen RE.

Nature. 2002 Sep 26;419(6905):403-7. Epub 2002 Sep 1.


Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-Cdk.

Verma R, McDonald H, Yates JR 3rd, Deshaies RJ.

Mol Cell. 2001 Aug;8(2):439-48.


Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome.

Guterman A, Glickman MH.

J Biol Chem. 2004 Jan 16;279(3):1729-38. Epub 2003 Oct 27.


In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome.

Amerik AYu, Swaminathan S, Krantz BA, Wilkinson KD, Hochstrasser M.

EMBO J. 1997 Aug 15;16(16):4826-38.


Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domain.

Rinaldi T, Pick E, Gambadoro A, Zilli S, Maytal-Kivity V, Frontali L, Glickman MH.

Biochem J. 2004 Jul 1;381(Pt 1):275-85.


Structure of the Jab1/MPN domain and its implications for proteasome function.

Tran HJ, Allen MD, Löwe J, Bycroft M.

Biochemistry. 2003 Oct 7;42(39):11460-5.


The 26S proteasome of the yeast Saccharomyces cerevisiae.

Fischer M, Hilt W, Richter-Ruoff B, Gonen H, Ciechanover A, Wolf DH.

FEBS Lett. 1994 Nov 21;355(1):69-75.


Proteasome assembly influences interaction with ubiquitinated proteins and shuttle factors.

Chandra A, Chen L, Liang H, Madura K.

J Biol Chem. 2010 Mar 12;285(11):8330-9. doi: 10.1074/jbc.M109.076786. Epub 2010 Jan 8.


An AAA Motor-Driven Mechanical Switch in Rpn11 Controls Deubiquitination at the 26S Proteasome.

Worden EJ, Dong KC, Martin A.

Mol Cell. 2017 Sep 7;67(5):799-811.e8. doi: 10.1016/j.molcel.2017.07.023. Epub 2017 Aug 24.


Integrity of the Saccharomyces cerevisiae Rpn11 protein is critical for formation of proteasome storage granules (PSG) and survival in stationary phase.

Saunier R, Esposito M, Dassa EP, Delahodde A.

PLoS One. 2013 Aug 6;8(8):e70357. doi: 10.1371/journal.pone.0070357. Print 2013.


Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome.

Elsasser S, Chandler-Militello D, Müller B, Hanna J, Finley D.

J Biol Chem. 2004 Jun 25;279(26):26817-22. Epub 2004 Apr 26.


Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome.

Papa FR, Amerik AY, Hochstrasser M.

Mol Biol Cell. 1999 Mar;10(3):741-56.


A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.

Glickman MH, Rubin DM, Coux O, Wefes I, Pfeifer G, Cjeka Z, Baumeister W, Fried VA, Finley D.

Cell. 1998 Sep 4;94(5):615-23.


Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome.

Bashore C, Dambacher CM, Goodall EA, Matyskiela ME, Lander GC, Martin A.

Nat Struct Mol Biol. 2015 Sep;22(9):712-9. doi: 10.1038/nsmb.3075. Epub 2015 Aug 24.


Cyclin-dependent kinase and Cks/Suc1 interact with the proteasome in yeast to control proteolysis of M-phase targets.

Kaiser P, Moncollin V, Clarke DJ, Watson MH, Bertolaet BL, Reed SI, Bailly E.

Genes Dev. 1999 May 1;13(9):1190-202.


The DOA pathway: studies on the functions and mechanisms of ubiquitin-dependent protein degradation in the yeast Saccharomyces cerevisiae.

Hochstrasser M, Papa FR, Chen P, Swaminathan S, Johnson P, Stillman L, Amerik AY, Li SJ.

Cold Spring Harb Symp Quant Biol. 1995;60:503-13. Review. No abstract available.


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