Gene Symbol: RPN10
Description: proteasome regulatory particle base subunit RPN10
Alias: MCB1, SUN1, proteasome regulatory particle base subunit RPN10
Species: Saccharomyces cerevisiae S288c
Products:     RPN10

Top Publications

  1. Ghaboosi N, Deshaies R. A conditional yeast E1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting Rad23 to the proteasome. Mol Biol Cell. 2007;18:1953-63 pubmed
    ..We propose that recognition of polyubiquitin chains by Rad23 promotes its shuttling to the proteasome in vivo. ..
  2. Koegl M, Hoppe T, Schlenker S, Ulrich H, Mayer T, Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell. 1999;96:635-44 pubmed
    ..In yeast, E4 activity is linked to cell survival under stress conditions, indicating that eukaryotes utilize E4-dependent proteolysis pathways for multiple cellular functions. ..
  3. Verma R, Oania R, Graumann J, Deshaies R. Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell. 2004;118:99-110 pubmed
    ..Genetic studies suggest a role for the multiubiquitin chain binding proteins (MCBPs) Rad23 and Rpn10 in recruitment, but biochemical studies implicate the Rpt5 ATPase...
  4. Xie Y, Varshavsky A. Physical association of ubiquitin ligases and the 26S proteasome. Proc Natl Acad Sci U S A. 2000;97:2497-502 pubmed
    ..These and related results suggest that a substrate-bound Ub ligase participates in the delivery of substrates to the proteasome, because of affinity between the ligase's E3 component and specific proteins of the 19S particle. ..
  5. 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
    ..Multiubiquitinated proteins interact with proteasome receptors, such as Rpn10, which intriguingly is also required for promoting proteasome stability...
  6. 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. ..
  7. 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
    ..Here we dissect the relationship of two proteasome-associated polyubiquitin-binding proteins, Rpn10 and Dsk2, and demonstrate how Rpn10 filters Dsk2 interactions, maintaining proper function of the ubiquitin-..
  8. 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. ..
  9. 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
    ..In addition, genetic interaction between SEM1 and RPN10 was detected...

More Information


  1. 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. ..
  2. 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
    ..Notably, Rpn11 moves from an occluded position to directly above the central pore, thus facilitating substrate deubiquitination concomitant with translocation. ..
  3. 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
    ..Expression of the carboxyl-terminal domain of Rpn11 partially suppressed the growth and proteasome stability defects of rpn11-1. These results indicate that ubiquitinated substrates are preferentially delivered to intact proteasome. ..
  4. Isasa M, Katz E, Kim W, Yugo V, González S, Kirkpatrick D, et al. Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome. Mol Cell. 2010;38:733-45 pubmed publisher
    The proteasome recognizes its substrates via a diverse set of ubiquitin receptors, including subunits Rpn10/S5a and Rpn13...
  5. 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. ..
  6. Rosenzweig R, Bronner V, Zhang D, Fushman D, Glickman M. Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome. J Biol Chem. 2012;287:14659-71 pubmed publisher
    ..Two neighboring subunits, Rpn10 and Rpn13, show a marked preference for polyubiquitin over UBLs...
  7. Attali I, Tobelaim W, Persaud A, Motamedchaboki K, Simpson Lavy K, Mashahreh B, et al. Ubiquitylation-dependent oligomerization regulates activity of Nedd4 ligases. EMBO J. 2017;36:425-440 pubmed publisher
    ..mechanism for Nedd4 ligases and demonstrated its function with diverse substrates: the yeast soluble proteins Rpn10 and Rvs167, and the human receptor tyrosine kinase FGFR1 and cardiac IKS potassium channel...
  8. Zhang D, Chen T, Ziv I, Rosenzweig R, Matiuhin Y, Bronner V, et al. Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor. Mol Cell. 2009;36:1018-33 pubmed publisher
    ..We obtained structural information on two receptors, Rpn10 and Dsk2, alone and in complex with (poly)ubiquitin or with each other...
  9. Crosas B, Hanna J, Kirkpatrick D, Zhang D, Tone Y, Hathaway N, et al. Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell. 2006;127:1401-13 pubmed
    ..We propose that through dynamic remodeling of ubiquitin chains, proteasomes actively regulate substrate commitment to degradation. ..
  10. 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
    ..We reported that Sts1 could suppress growth and proteolytic defects of rad23? rpn10?. We show here that Sts1 suppresses a previously undetected proteasome localization defect in this mutant...
  11. Takeuchi J, Fujimuro M, Yokosawa H, Tanaka K, Toh e A. Rpn9 is required for efficient assembly of the yeast 26S proteasome. Mol Cell Biol. 1999;19:6575-84 pubmed
    We have isolated the RPN9 gene by two-hybrid screening with, as bait, RPN10 (formerly SUN1), which encodes a multiubiquitin chain receptor residing in the regulatory particle of the 26S proteasome...
  12. Lambertson D, Chen L, Madura K. Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae. Genetics. 1999;153:69-79 pubmed
    ..Similarly, a small fraction of Rpn10 is a component of the proteasome...
  13. Keren Kaplan T, Prag G. Purification and crystallization of mono-ubiquitylated ubiquitin receptor Rpn10. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012;68:1120-3 pubmed publisher
    ..coli was used to purify the mono-ubiquitylated form of the regulatory proteasomal non-ATPase subunit (Ub-Rpn10) from Saccharomyces cerevisiae. Here, the first crystallization and data collection of Ub-Rpn10 is reported...
  14. Chuang S, Chen L, Lambertson D, Anand M, Kinzy T, Madura K. Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A. Mol Cell Biol. 2005;25:403-13 pubmed
    Rad23 and Rpn10 play synergistic roles in the recognition of ubiquitinated proteins by the proteasome, and loss of both proteins causes growth and proteolytic defects...
  15. Mayor T, Graumann J, Bryan J, MacCoss M, Deshaies R. Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway. Mol Cell Proteomics. 2007;6:1885-95 pubmed
    ..To address how broad of a role the ubiquitin receptor Rpn10 (S5a) plays in turnover of proteasome substrates, we implemented a method to perform quantitative analysis of ..
  16. Imai J, Maruya M, Yashiroda H, Yahara I, Tanaka K. The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J. 2003;22:3557-67 pubmed
    ..Our results indicate that Hsp90 interacts with the 26S proteasome and plays a principal role in the assembly and maintenance of the 26S proteasome. ..
  17. Cortajarena A, Liu T, Hochstrasser M, Regan L. Designed proteins to modulate cellular networks. ACS Chem Biol. 2010;5:545-52 pubmed publisher
    ..Furthermore, we demonstrated that these modules inhibit Sem1 activity in yeast. This strategy will be generally applicable to make novel genetically encoded tools for systems/synthetic biology applications. ..
  18. 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. ..
  19. Chen L, Madura K. Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol Cell Biol. 2002;22:4902-13 pubmed
    ..Rad23 plays an overlapping role with Rpn10, a proteasome-associated multi-Ub chain binding protein...
  20. Puig Sàrries P, Bijlmakers M, Zuin A, Bichmann A, Pons M, Crosas B. An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination. Biochem J. 2015;469:455-67 pubmed publisher
    ..We present here the analysis of the process of monoubiquitination of the proteasomal subunit Rpn10 (regulatory particle non-ATPase 10), involved in the recruitment of polyubiquitinated substrates...
  21. Laribee R, Shibata Y, Mersman D, Collins S, Kemmeren P, Roguev A, et al. CCR4/NOT complex associates with the proteasome and regulates histone methylation. Proc Natl Acad Sci U S A. 2007;104:5836-41 pubmed
    ..These studies implicate CCR4/NOT in the regulation of H3K4me3 through a ubiquitin-dependent pathway that likely involves the proteasome. ..
  22. Romero Perez L, Chen L, Lambertson D, Madura K. Sts1 can overcome the loss of Rad23 and Rpn10 and represents a novel regulator of the ubiquitin/proteasome pathway. J Biol Chem. 2007;282:35574-82 pubmed
    ..Despite these proteolytic defects, overall proteasome activity was increased in sts1-2. We propose that Sts1 is a new regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates...
  23. Yashiroda H, Mizushima T, Okamoto K, Kameyama T, Hayashi H, Kishimoto T, et al. Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. Nat Struct Mol Biol. 2008;15:228-36 pubmed publisher
    ..The structure of the Dmp1-Dmp2-alpha5 complex reveals how this chaperone functions in proteasome assembly and why it dissociates from proteasome precursors before the beta-rings are assembled. ..
  24. 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. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. ..
  25. Le Tallec B, Barrault M, Guerois R, Carré T, Peyroche A. Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome. Mol Cell. 2009;33:389-99 pubmed publisher
    ..Finally, we identify the putative species-specific 19S subunit S5b as a functional homolog of the Hsm3 chaperone in mammals. These findings shed light on chaperone-assisted proteasome assembly in eukaryotes. ..
  26. Richly H, Rape M, Braun S, Rumpf S, Hoege C, Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell. 2005;120:73-84 pubmed
    ..In yeast, this escort pathway guides a transcription factor from its activation in the cytosol to its final degradation and also mediates proteolysis at the endoplasmic reticulum by the ERAD pathway. ..
  27. Fujimuro M, Tanaka K, Yokosawa H, Toh e A. Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett. 1998;423:149-54 pubmed
    ..The resultant precipitate contained Nin1p, Sun1p, TBP1, and the 20S proteasome. Combining genetic and biochemical results together, we concluded that Son1p is a component of the yeast 26S proteasome. ..
  28. Schuberth C, Richly H, Rumpf S, Buchberger A. Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation. EMBO Rep. 2004;5:818-24 pubmed
    ..Our data suggest that Shp1 and Ubx2 are adaptors for Cdc48-dependent protein degradation through the ubiquitin/proteasome pathway. ..
  29. 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
    ..majority (if not all) of the double-capped 26S proteasomes, both 19S complexes, contain the ubiquitin receptor Rpn10/S5a, only one of these 19S particles contains the additional ubiquitin receptor Rpn13, thereby defining asymmetry ..
  30. Heessen S, Masucci M, Dantuma N. The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation. Mol Cell. 2005;18:225-35 pubmed
    ..a mutant Rad23 that lacks a functional UBA2 domain shows increased sensitivity to UV light and, in the absence of Rpn10, severe growth defects...
  31. Le Tallec B, Barrault M, Courbeyrette R, Guerois R, Marsolier Kergoat M, Peyroche A. 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol Cell. 2007;27:660-74 pubmed
    ..Our findings provide evidence for a remarkable conservation of a pairwise chaperone-assisted proteasome assembly throughout evolution. ..
  32. Voloshin O, Gocheva Y, Gutnick M, Movshovich N, Bakhrat A, Baranes Bachar K, et al. Tubulin chaperone E binds microtubules and proteasomes and protects against misfolded protein stress. Cell Mol Life Sci. 2010;67:2025-38 pubmed publisher
    ..Pac2 binds proteasomes: the LRR binds Rpn1, and the UbL binds Rpn10; the latter interaction mediates Pac2 turnover...
  33. Sakata E, Bohn S, Mihalache O, Kiss P, Beck F, Nagy I, et al. Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy. Proc Natl Acad Sci U S A. 2012;109:1479-84 pubmed publisher
    Two canonical subunits of the 26S proteasome, Rpn10 and Rpn13, function as ubiquitin (Ub) receptors. The mutual arrangement of these subunits--and all other non-ATPase subunits--in the regulatory particle is unknown...
  34. 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
    Despite the progress made in understanding the roles of proteasome polyubiquitin receptors, such as the subunits Rpn10 (regulatory particle non-ATPase 10) and Rpn13, and the transient interactors Rad23 (radiation sensitivity abnormal 23) ..
  35. 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
    ..Recent genetic studies showed that Rpn11 is functionally linked to Rpn10, a major multiubiquitin chain binding receptor in the proteasome...
  36. Keren Kaplan T, Attali I, Motamedchaboki K, Davis B, Tanner N, Reshef Y, et al. Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria. EMBO J. 2012;31:378-90 pubmed publisher
    ..Contrary to in-vitro assays that lead to spurious modification of several lysine residues of Rpn10 (regulatory proteasomal non-ATPase subunit), the reconstituted system faithfully recapitulates its ..
  37. Laribee R, Krogan N, Xiao T, Shibata Y, Hughes T, Greenblatt J, et al. BUR kinase selectively regulates H3 K4 trimethylation and H2B ubiquitylation through recruitment of the PAF elongation complex. Curr Biol. 2005;15:1487-93 pubmed
    ..Our data reveal a novel function for the BUR kinase in transcriptional regulation through the selective control of histone modifications. ..
  38. Kim H, Kim K, Uchiki T, Gygi S, Goldberg A. S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains. EMBO J. 2009;28:1867-77 pubmed publisher
    ..Thus, S5a (and presumably certain other UIM proteins) function with certain E3/E2 pairs to ensure synthesis of efficiently degraded non-forked Ub conjugates. ..
  39. 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
    ..ubiquitin-shuttle proteins comparably to ubiquitin but binds more weakly to a proteasomal ubiquitin receptor Rpn10. We identified Rub1-ubiquitin heteromers in yeast and Nedd8-Ub heteromers in human cells...
  40. 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. ..
  41. Elsasser S, Chandler Militello D, Müller B, Hanna J, Finley D. Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J Biol Chem. 2004;279:26817-22 pubmed
    ..Here we show that the proteasome directly recognizes ubiquitin chains through a specific subunit, Rpn10, and also recognizes chains indirectly through Rad23, a reversibly bound proteasome cofactor...
  42. 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
  43. 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. ..
  44. Keren Kaplan T, Zeev Peters L, Levin Kravets O, Attali I, Kleifeld O, Shohat N, et al. Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism. Nat Commun. 2016;7:12960 pubmed publisher
    ..a ubiquitylation apparatus, we purified and determined the crystal structure of the proteasomal ubiquitin-receptor Rpn10 in its ubiquitylated state. The structure shows a novel ubiquitin-binding patch that directs K84 ubiquitylation...
  45. 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. ..
  46. Rubin D, van Nocker S, Glickman M, Coux O, Wefes I, Sadis S, et al. ATPase and ubiquitin-binding proteins of the yeast proteasome. Mol Biol Rep. 1997;24:17-26 pubmed
    ..We have also found that the multiubiquitin chain binding protein Mcb1, a homolog of the mammalian S5a protein, is a subunit of the yeast proteasome...
  47. Rani N, Aichem A, Schmidtke G, Kreft S, Groettrup M. FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis. Nat Commun. 2012;3:749 pubmed publisher
    ..We identify the 26S proteasome subunit hRpn10/S5a as the receptor for FAT10, whereas NUB1L can bind to both Rpn10 and Rpn1/S2. Unexpectedly, FAT10 and NUB1L both interact with hRpn10 via the VWA domain...
  48. Fatimababy A, Lin Y, Usharani R, Radjacommare R, Wang H, Tsai H, et al. Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis. FEBS J. 2010;277:796-816 pubmed publisher
    ..of ubiquitin/26S proteasome-mediated proteolysis (UPP), which is mediated directly by the proteasome subunit RPN10 and/or RPN13, or indirectly by ubiquitin receptors containing ubiquitin-like and ubiquitin-associated domains...
  49. 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. ..
  50. Kirkpatrick D, Hathaway N, Hanna J, Elsasser S, Rush J, Finley D, et al. Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology. Nat Cell Biol. 2006;8:700-10 pubmed
    ..Together, our observations expand the context of what can be considered to be a sufficient degradation signal and provide unique insights into the mechanisms of substrate ubiquitination. ..
  51. Verma R, Peters N, D Onofrio M, Tochtrop G, Sakamoto K, Varadan R, et al. Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain. Science. 2004;306:117-20 pubmed
    ..The same interface is recognized by ubiquitin-chain receptors of the proteasome, indicating that ubistatins act by disrupting a critical protein-protein interaction in the ubiquitin-proteasome system. ..
  52. Saeki Y, Saitoh A, Toh e A, Yokosawa H. Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun. 2002;293:986-92 pubmed
    b>Rpn10, a subunit of the 26S proteasome, has been proposed to act as a receptor for multiubiquitin chains in ubiquitin-dependent proteolysis...
  53. Mitchell D, Hamel L, Ishizuka K, Mitchell G, Schaefer L, Deschenes R. The Erf4 subunit of the yeast Ras palmitoyl acyltransferase is required for stability of the Acyl-Erf2 intermediate and palmitoyl transfer to a Ras2 substrate. J Biol Chem. 2012;287:34337-48 pubmed publisher
    ..This is the first demonstration of regulation of a DHHC PAT enzyme by an associated protein. ..
  54. 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. ..
  55. Hu Y, Wu Y, Li Q, Zhang W, Jin C. Solution structure of yeast Rpn9: insights into proteasome lid assembly. J Biol Chem. 2015;290:6878-89 pubmed publisher
    ..The N-terminal domain mediates interaction with the ubiquitin receptor Rpn10, whereas the PCI domain mediates interaction with the neighboring PCI subunit Rpn5...
  56. Ishii T, Funakoshi M, Kobayashi H. Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway. EMBO J. 2006;25:5492-503 pubmed
    ..Pth2 inhibited the interaction of Rad23 and Dsk2 with the polyubiquitin receptors Rpn1 and Rpn10 on the proteasome...
  57. Shi Y, Chen X, Elsasser S, Stocks B, Tian G, Lee B, et al. Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome. Science. 2016;351: pubmed publisher
    ..Thus, a two-site recognition domain intrinsic to the proteasome uses distinct ubiquitin-fold ligands to assemble substrates, shuttling factors, and a deubiquitinating enzyme. ..
  58. 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 ..
  59. Gödderz D, Giovannucci T, Lalakova J, Menendez Benito V, Dantuma N. The deubiquitylating enzyme Ubp12 regulates Rad23-dependent proteasomal degradation. J Cell Sci. 2017;130:3336-3346 pubmed publisher
    ..Our data suggest that ubiquitylation of Rad23 plays a stimulatory role in the degradation of ubiquitylated substrates by the proteasome. ..
  60. Funakoshi M, Li X, Velichutina I, Hochstrasser M, Kobayashi H. Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability. J Cell Sci. 2004;117:6447-54 pubmed
    ..impairs the stability of the 26S proteasome and sem1Delta defects are greatly enhanced by simultaneous deletion of RPN10. The Rpn10 proteasome subunit appears to function with Sem1 in maintaining the association of the lid and base ..
  61. van Nocker S, Sadis S, Rubin D, Glickman M, Fu H, Coux O, et al. The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol Cell Biol. 1996;16:6020-8 pubmed
    ..In this study, we identified a Saccharomyces cerevisiae homolog of this protein, designated Mcb1. Mcb1 copurified with the 26S proteasome in both conventional and nickel chelate chromatography...