RPN11

Summary

Gene Symbol: RPN11
Description: proteasome regulatory particle lid subunit RPN11
Alias: MPR1, proteasome regulatory particle lid subunit RPN11
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Rinaldi T, Hofmann L, Gambadoro A, Cossard R, Livnat Levanon N, Glickman M, et al. Dissection of the carboxyl-terminal domain of the proteasomal subunit Rpn11 in maintenance of mitochondrial structure and function. Mol Biol Cell. 2008;19:1022-31 pubmed publisher
    We have previously demonstrated that the C-terminal part of Rpn11, a deubiquitinating enzyme in the lid of the proteasome, is essential for maintaining a correct cell cycle and normal mitochondrial morphology and function...
  2. Tomko R, Hochstrasser M. Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining. Mol Cell. 2011;44:907-17 pubmed publisher
    ..Rpn12 incorporation thus links proper lid assembly to subsequent assembly steps. ..
  3. Matyskiela M, Lander G, Martin A. Conformational switching of the 26S proteasome enables substrate degradation. Nat Struct Mol Biol. 2013;20:781-8 pubmed publisher
    ..Its regulatory particle, containing the heterohexameric AAA+ ATPase motor and the essential deubiquitinase Rpn11, recognizes substrates, removes their ubiquitin chains and translocates them into the associated peptidase after ..
  4. Yao T, Cohen R. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature. 2002;419:403-7 pubmed
    ..Here we report that the POH1 (also known as Rpn11 in yeast) subunit of the 19S complex is responsible for substrate deubiquitination during proteasomal degradation...
  5. Estrin E, Lopéz Blanco J, Chacon P, Martin A. Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid. Structure. 2013;21:1624-35 pubmed publisher
    ..Finally, we predict that the assembly of the COP9 signalosome depends on a similar helical bundle. ..
  6. Glickman M, Rubin D, Fried V, Finley D. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol. 1998;18:3149-62 pubmed
    ..Overall, regulatory particles from yeasts and mammals are remarkably similar, suggesting that the specific mechanistic features of the proteasome have been closely conserved over the course of evolution. ..
  7. Chandra A, Chen L, Madura K. Synthetic lethality of rpn11-1 rpn10? is linked to altered proteasome assembly and activity. Curr Genet. 2010;56:543-57 pubmed publisher
    An rpn11-1 temperature-sensitive mutant shows defect in proteolysis, mitochondrial function and proteasome assembly. The Rpn11 protein is a proteasome subunit that deubiquitinates proteolytic substrates...
  8. Funakoshi M, Tomko R, Kobayashi H, Hochstrasser M. Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell. 2009;137:887-99 pubmed publisher
    ..Our results demonstrate that proteasomal RP biogenesis requires multiple, functionally overlapping chaperones and suggest a model in which subunits form specific subcomplexes that then assemble into the base. ..
  9. Laporte D, Salin B, Daignan Fornier B, Sagot I. Reversible cytoplasmic localization of the proteasome in quiescent yeast cells. J Cell Biol. 2008;181:737-45 pubmed publisher
    ..Finally, we observe conserved formation and mobilization of these PSGs in the evolutionary distant yeast Schizosaccharomyces pombe. This conservation implies a broad significance for these proteasome reserves. ..

More Information

Publications62

  1. Wendler P, Lehmann A, Janek K, Baumgart S, Enenkel C. The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin alphabeta and proteasome functions. J Biol Chem. 2004;279:37751-62 pubmed
    ..Our data support the model by which nuclear 26 S proteasomes are assembled from subcomplexes imported by karyopherin alphabeta. ..
  2. Verma R, Aravind L, Oania R, McDonald W, Yates J, Koonin E, et al. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science. 2002;298:611-5 pubmed
    ..The Rpn11 subunit of the proteasome lid subcomplex contains a highly conserved Jab1/MPN domain-associated ..
  3. Pathare G, Nagy I, Sledź P, Anderson D, Zhou H, Pardon E, et al. Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11. Proc Natl Acad Sci U S A. 2014;111:2984-9 pubmed publisher
    ..substrates is preceded by the removal of polyubiquitin moieties through the isopeptidase activity of the subunit Rpn11. Here we describe three crystal structures of the heterodimer of the Mpr1-Pad1-N-terminal domains of Rpn8 and ..
  4. Worden E, Padovani C, Martin A. Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation. Nat Struct Mol Biol. 2014;21:220-7 pubmed publisher
    Polyubiquitin chains target protein substrates to the 26S proteasome, where they are removed by the deubiquitinase Rpn11 to allow efficient substrate degradation...
  5. Chandra A, Chen L, Liang H, Madura K. Proteasome assembly influences interaction with ubiquitinated proteins and shuttle factors. J Biol Chem. 2010;285:8330-9 pubmed publisher
    ..Enzymes, such as Rpn11, dismantle multiubiquitin chains, and mutations can affect proteasome assembly and activity...
  6. Hofmann L, Saunier R, Cossard R, Esposito M, Rinaldi T, Delahodde A. A nonproteolytic proteasome activity controls organelle fission in yeast. J Cell Sci. 2009;122:3673-83 pubmed publisher
    ..are not controlled by the proteasome activity but rather depend on a new function of the proteasomal lid subunit Rpn11. Rpn11 was found to regulate the Fis1-dependent fission machinery of both organelles...
  7. Sone T, Saeki Y, Toh e A, Yokosawa H. Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae. J Biol Chem. 2004;279:28807-16 pubmed
    ..The results suggest that Sem1, possibly hDSS1, is a novel subunit of the 26 S proteasome and plays a role in ubiquitin-dependent proteolysis. ..
  8. Lander G, Estrin E, Matyskiela M, Bashore C, Nogales E, Martin A. Complete subunit architecture of the proteasome regulatory particle. Nature. 2012;482:186-91 pubmed publisher
    ..We provide a structural basis for the ability of the proteasome to degrade a diverse set of substrates and thus regulate vital cellular processes. ..
  9. Leggett D, Hanna J, Borodovsky A, Crosas B, Schmidt M, Baker R, et al. Multiple associated proteins regulate proteasome structure and function. Mol Cell. 2002;10:495-507 pubmed
    ..ubp6Delta mutants exhibit accelerated turnover of ubiquitin, indicating that deubiquitination events catalyzed by Ubp6 prevent translocation of ubiquitin into the proteolytic core particle. ..
  10. Tomko R, Hochstrasser M. The intrinsically disordered Sem1 protein functions as a molecular tether during proteasome lid biogenesis. Mol Cell. 2014;53:433-43 pubmed publisher
    ..Thus, although Sem1 is a stoichiometric component of the mature proteasome, it has a distinct, chaperone-like function specific to early stages of proteasome assembly. ..
  11. Matiuhin Y, Kirkpatrick D, Ziv I, Kim W, Dakshinamurthy A, Kleifeld O, et al. Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome. Mol Cell. 2008;32:415-25 pubmed publisher
    ..This work highlights the importance of polyubiquitin shuttles such as Rpn10 and Dsk2 in controlling the ubiquitin landscape. ..
  12. Rinaldi T, Pick E, Gambadoro A, Zilli S, Maytal Kivity V, Frontali L, et al. Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domain. Biochem J. 2004;381:275-85 pubmed
    Substrates destined for degradation by the 26 S proteasome are labelled with polyubiquitin chains. Rpn11/Mpr1, situated in the lid subcomplex, partakes in the processing of these chains or in their removal from substrates bound to the ..
  13. Hibi T, Yamamoto H, Nakamura G, Takagi H. Crystallization and preliminary crystallographic analysis of N-acetyltransferase Mpr1 from Saccharomyces cerevisiae. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009;65:169-72 pubmed publisher
    b>Mpr1 is an enzyme that catalyzes the N-acetylation of the toxic L-azetidine-2-carboxylic acid (AZC). Recently, Mpr1 has been shown to reduce levels of intracellular reactive oxygen species (ROS) under oxidative stress...
  14. Seong K, Baek J, Ahn B, Yu M, Kim J. Rpn10p is a receptor for ubiquitinated Gcn4p in proteasomal proteolysis. Mol Cells. 2007;24:194-9 pubmed
    ..These results suggest that Rpn10p is the receptor that binds the polyubiquitin chain during ubiquitin-dependent proteolysis of Gcn4p. ..
  15. Verma R, Oania R, Fang R, Smith G, Deshaies R. Cdc48/p97 mediates UV-dependent turnover of RNA Pol II. Mol Cell. 2011;41:82-92 pubmed publisher
    ..These data reveal an intimate coupling of function between proteasomes and Cdc48 that we suggest is necessary to sustain processive degradation of unstable subunits of some macromolecular protein complexes. ..
  16. Isono E, Saeki Y, Yokosawa H, Toh e A. Rpn7 Is required for the structural integrity of the 26 S proteasome of Saccharomyces cerevisiae. J Biol Chem. 2004;279:27168-76 pubmed
    ..From these results, we concluded that Rpn7 is required for the integrity of the 26 S complex by establishing a correct lid structure. ..
  17. Chen L, Romero L, Chuang S, Tournier V, Joshi K, Lee J, et al. Sts1 plays a key role in targeting proteasomes to the nucleus. J Biol Chem. 2011;286:3104-18 pubmed publisher
    ..Taken together, these findings explain the suppression of rad23? rpn10? by Sts1 and suggest that the degradation of nuclear substrates requires efficient proteasome localization. ..
  18. Berko D, Herkon O, Braunstein I, Isakov E, David Y, Ziv T, et al. Inherent asymmetry in the 26S proteasome is defined by the ubiquitin receptor RPN13. J Biol Chem. 2014;289:5609-18 pubmed publisher
    ..Our data point to a potential new role for ubiquitin receptors as directionality factors that may participate in the prevention of simultaneous substrates translocation into the 20S from both 19S caps...
  19. Taverner T, Hernandez H, Sharon M, Ruotolo B, Matak Vinkovic D, Devos D, et al. Subunit architecture of intact protein complexes from mass spectrometry and homology modeling. Acc Chem Res. 2008;41:617-27 pubmed publisher
    ..Overall therefore this mass spectrometry and homology modeling approach has given significant insight into the structure of two previously intractable protein complexes and as such has broad application in structural biology. ..
  20. Esposito M, Piatti S, Hofmann L, Frontali L, Delahodde A, Rinaldi T. Analysis of the rpn11-m1 proteasomal mutant reveals connection between cell cycle and mitochondrial biogenesis. FEMS Yeast Res. 2011;11:60-71 pubmed publisher
    The proteasomal lid subunit Rpn11 is essential for maintaining a correct cell cycle and mitochondrial morphology in Saccharomyces cerevisiae...
  21. Joshi K, Chen L, Torres N, Tournier V, Madura K. A proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress. J Mol Biol. 2011;410:383-99 pubmed publisher
    b>Rpn11 is a proteasome-associated deubiquitinating enzyme that is essential for viability. Recent genetic studies showed that Rpn11 is functionally linked to Rpn10, a major multiubiquitin chain binding receptor in the proteasome...
  22. Guterman A, Glickman M. Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. J Biol Chem. 2004;279:1729-38 pubmed
    ..In agreement, we find that highly purified proteasomes contain both Rpn11 and Ubp6, situated within the lid and base subcomplexes, respectively...
  23. Saeki Y, Isono E, Toh e A. Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity. Methods Enzymol. 2005;399:215-27 pubmed
    ..In this communication, we describe that Sic1 was successfully ubiquitinated by the PY motif-insertion method and demonstrate that Sic1 thus ubiquitinated was degraded by the purified yeast 26S proteasome. ..
  24. Kotani T, Takagi H. Identification of amino acid residues essential for the yeast N-acetyltransferase Mpr1 activity by site-directed mutagenesis. FEMS Yeast Res. 2008;8:607-14 pubmed publisher
    We previously discovered that the budding yeast Saccharomyces cerevisiae Sigma1278b has the MPR1 gene that confers resistance to the proline analogue azetidine-2-carboxylate (AZC)...
  25. Dambacher C, Worden E, Herzik M, Martin A, Lander G. Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition. elife. 2016;5:e13027 pubmed publisher
    ..from targeted substrates at the proteasome is a prerequisite for substrate processing and is accomplished by Rpn11, a deubiquitinase within the 'lid' sub-complex...
  26. Nishimura A, Kotani T, Sasano Y, Takagi H. An antioxidative mechanism mediated by the yeast N-acetyltransferase Mpr1: oxidative stress-induced arginine synthesis and its physiological role. FEMS Yeast Res. 2010;10:687-98 pubmed publisher
    Saccharomyces cerevisiaeSigma1278b has the MPR1 gene encoding the N-acetyltransferase Mpr1 that acetylates the proline metabolism intermediate Delta(1)-pyrroline-5-carboxylate (P5C)/glutamate-gamma-semialdehyde (GSA) in vitro...
  27. Yashiroda H, Toda Y, Otsu S, Takagi K, Mizushima T, Murata S. N-terminal α7 deletion of the proteasome 20S core particle substitutes for yeast PI31 function. Mol Cell Biol. 2015;35:141-52 pubmed publisher
    ..These results suggest that the α7 N terminus has a role in CP activation different from that of the α3 N terminus and that the role of Fub1 antagonizes a specific function of the α7 N terminus. ..
  28. Singh R, Zerath S, Kleifeld O, Scheffner M, Glickman M, Fushman D. Recognition and cleavage of related to ubiquitin 1 (Rub1) and Rub1-ubiquitin chains by components of the ubiquitin-proteasome system. Mol Cell Proteomics. 2012;11:1595-611 pubmed publisher
    ..Taken together, these findings suggest that once Rub1/Nedd8 is channeled into ubiquitin pathways, it is recognized essentially like ubiquitin. ..
  29. Worden E, Dong K, Martin A. An AAA Motor-Driven Mechanical Switch in Rpn11 Controls Deubiquitination at the 26S Proteasome. Mol Cell. 2017;67:799-811.e8 pubmed publisher
    ..Poly-ubiquitin chains direct protein substrates to the 26S proteasome, where they are removed by the deubiquitinase Rpn11 during ATP-dependent substrate degradation...
  30. Kalies K, Allan S, Sergeyenko T, Kroger H, Römisch K. The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane. EMBO J. 2005;24:2284-93 pubmed
    ..Collectively, our data suggest that the Sec61 channel is a principal proteasome receptor in the ER membrane. ..
  31. Pribylova L, Sychrova H. Expression of the Saccharomyces cerevisiae MPR1 gene encoding N-acetyltransferase in Zygosaccharomyces rouxii confers resistance to L-azetidine-2-carboxylate. Folia Microbiol (Praha). 2006;51:203-7 pubmed
    ..The possibility of use of the Saccharomyces cerevisiae MPR1 gene (ScMPR1) encoding the AZC-detoxifying enzyme as a dominant selection marker in Z. rouxii was examined...
  32. Saeki Y, Kudo T, Sone T, Kikuchi Y, Yokosawa H, Toh e A, et al. Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome. EMBO J. 2009;28:359-71 pubmed publisher
    ..These results raise the possibility that Lys63-linked ubiquitin chain also serves as a targeting signal for the 26S proteaseome in vivo. ..
  33. Schaefer J, Morgan D. Protein-linked ubiquitin chain structure restricts activity of deubiquitinating enzymes. J Biol Chem. 2011;286:45186-96 pubmed publisher
    ..We propose that the resistance to many DUBs of long, substrate-attached Lys(48)-linked chains helps ensure that proteins are maintained free from ubiquitin until a threshold of ubiquitin ligase activity enables degradation...
  34. Ding Z, Fu Z, Xu C, Wang Y, Wang Y, Li J, et al. High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx. Cell Res. 2017;27:373-385 pubmed publisher
    ..Our results provide new insights into the mechanisms of nucleotide-driven allosteric cooperativity of the complex and of the substrate processing by the proteasome. ..
  35. Tomko R, Taylor D, Chen Z, Wang H, Rappsilber J, Hochstrasser M. A Single α Helix Drives Extensive Remodeling of the Proteasome Lid and Completion of Regulatory Particle Assembly. Cell. 2015;163:432-44 pubmed publisher
    ..Such assembly-coupled conformational switching is reminiscent of viral particle maturation and may represent a commonly used mechanism to enforce hierarchical assembly in multisubunit complexes. ..
  36. Mansour W, Nakasone M, von Delbrück M, Yu Z, Krutauz D, Reis N, et al. Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6. J Biol Chem. 2015;290:4688-704 pubmed publisher
    ..We characterized the specificities of two proteasome-associated deubiquitinases (DUBs), Rpn11 and Ubp6, and explored their impact on overall proteasome DUB activity...
  37. Luan B, Huang X, Wu J, Mei Z, Wang Y, Xue X, et al. Structure of an endogenous yeast 26S proteasome reveals two major conformational states. Proc Natl Acad Sci U S A. 2016;113:2642-7 pubmed publisher
    ..Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid...
  38. Yu Z, Livnat Levanon N, Kleifeld O, Mansour W, Nakasone M, Castaneda C, et al. Base-CP proteasome can serve as a platform for stepwise lid formation. Biosci Rep. 2015;35: pubmed publisher
    ..Even within the lid, subunits have been demarcated into two modules: module 1 (Rpn5, Rpn6, Rpn8, Rpn9 and Rpn11), which interacts with both CP and base sub-complexes and module 2 (Rpn3, Rpn7, Rpn12 and Rpn15) that is attached ..
  39. De La Mota Peynado A, Lee S, Pierce B, Wani P, Singh C, Roelofs J. The proteasome-associated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the proteasome. J Biol Chem. 2013;288:29467-81 pubmed publisher
    ..We propose that the inhibitory ability of Ecm29 is important for its function as a proteasome quality control factor by ensuring that aberrant proteasomes recognized by Ecm29 are inactive. ..
  40. Voloshin O, Bakhrat A, Herrmann S, Raveh D. Transfer of Ho endonuclease and Ufo1 to the proteasome by the UbL-UbA shuttle protein, Ddi1, analysed by complex formation in vitro. PLoS ONE. 2012;7:e39210 pubmed publisher
    ..Our interpretation is that in the absence of substrate, the Ddi1-UbL binds Rpn1 while the Ddi1-UbA binds ubiquitin chains on Ufo1. This would promote degradation of Ufo1 and disassembly of SCF(Ufo1) complexes. ..
  41. Prasanth K, Barajas D, Nagy P. The proteasomal Rpn11 metalloprotease suppresses tombusvirus RNA recombination and promotes viral replication via facilitating assembly of the viral replicase complex. J Virol. 2015;89:2750-63 pubmed publisher
    ..Overexpression of Ded1p can complement the defect observed in rpn11 mutant yeast by reducing TBSV recombination...
  42. Saunier R, Esposito M, Dassa E, Delahodde A. Integrity of the Saccharomyces cerevisiae Rpn11 protein is critical for formation of proteasome storage granules (PSG) and survival in stationary phase. PLoS ONE. 2013;8:e70357 pubmed publisher
    ..We showed that a particular mutant of the RPN11 gene (rpn11-m1), encoding a proteasome lid subunit already known to exhibit proteasome assembly/stability defect ..
  43. Zuin A, Bichmann A, Isasa M, Puig Sàrries P, Díaz L, Crosas B. Rpn10 monoubiquitination orchestrates the association of the ubiquilin-type DSK2 receptor with the proteasome. Biochem J. 2015;472:353-65 pubmed publisher
    ..Interestingly, Rpn10-ubiquitin, with an inactivated ubiquitin-interacting motif (UIM), and Dsk2(I45S), with an inactive ubiquitin-like domain (UBL), show temperature-dependent phenotypes with multiple functional interactions. ..
  44. Mao P, Smerdon M. Yeast deubiquitinase Ubp3 interacts with the 26 S proteasome to facilitate Rad4 degradation. J Biol Chem. 2010;285:37542-50 pubmed publisher
  45. Saeki Y, Toh e A, Kudo T, Kawamura H, Tanaka K. Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle. Cell. 2009;137:900-13 pubmed publisher
    ..Our results indicate that the RP assembly is a highly organized and elaborate process orchestrated by multiple proteasome-dedicated chaperones. ..
  46. Kimura Y, Saeki Y, Yokosawa H, Polevoda B, Sherman F, Hirano H. N-Terminal modifications of the 19S regulatory particle subunits of the yeast proteasome. Arch Biochem Biophys. 2003;409:341-8 pubmed
    ..subunits, Rpt4, Rpt5, Rpt6, Rpn2, Rpn3, Rpn5, Rpn6, and Rpn8, were NatA substrates, and that 2 subunits, Rpt3 and Rpn11, were NatB substrates...
  47. Peters L, Karmon O, David Kadoch G, Hazan R, Yu T, Glickman M, et al. The protein quality control machinery regulates its misassembled proteasome subunits. PLoS Genet. 2015;11:e1005178 pubmed publisher
    ..Thus, we show that proteasome homeostasis is controlled through probing the level of proteasome assembly, and the interplay between UPS mediated degradation or their sorting into distinct cellular compartments. ..
  48. Wang X, Yen J, Kaiser P, Huang L. Regulation of the 26S proteasome complex during oxidative stress. Sci Signal. 2010;3:ra88 pubmed publisher
  49. Isasa M, Suñer C, Díaz M, Puig Sàrries P, Zuin A, Bichman A, et al. Cold Temperature Induces the Reprogramming of Proteolytic Pathways in Yeast. J Biol Chem. 2016;291:1664-75 pubmed publisher
    ..These unanticipated observations indicate that, during cold response, there is a proteolytic cellular reprogramming in which the proteasome acquires a role in the endocytic-vacuolar pathway. ..
  50. Tabb M, Tongaonkar P, Vu L, Nomura M. Evidence for separable functions of Srp1p, the yeast homolog of importin alpha (Karyopherin alpha): role for Srp1p and Sts1p in protein degradation. Mol Cell Biol. 2000;20:6062-73 pubmed
    ..b>RPN11 and STS1 (DBF8) were identified as high-dosage suppressors of the srp1-49 mutation but not of the srp1-31 mutation...
  51. Nasuno R, Hirano Y, Itoh T, Hakoshima T, Hibi T, Takagi H. Structural and functional analysis of the yeast N-acetyltransferase Mpr1 involved in oxidative stress tolerance via proline metabolism. Proc Natl Acad Sci U S A. 2013;110:11821-6 pubmed publisher
    b>Mpr1 (sigma1278b gene for proline-analog resistance 1), which was originally isolated as N-acetyltransferase detoxifying the proline analog L-azetidine-2-carboxylate, protects yeast cells from various oxidative stresses...
  52. Saeki Y, Toh e A, Yokosawa H. Rapid isolation and characterization of the yeast proteasome regulatory complex. Biochem Biophys Res Commun. 2000;273:509-15 pubmed
    ..In contrast with the previously reported result showing that Rpn10, a multiubiquitin chain binding subunit, is a component of the base complex, we present evidence that the lid complex isolated from wild-type yeast contains Rpn10. ..
  53. Sokolova V, Li F, Polovin G, Park S. Proteasome Activation is Mediated via a Functional Switch of the Rpt6 C-terminal Tail Following Chaperone-dependent Assembly. Sci Rep. 2015;5:14909 pubmed publisher
    ..Together, our data support the reported role of Rpt6 during proteasome assembly, and suggest that its function switches from anchoring for RP assembly into promoting Rpt3-dependent activation of the mature proteasome. ..