RPN1

Summary

Gene Symbol: RPN1
Description: proteasome regulatory particle base subunit RPN1
Alias: HRD2, NAS1, proteasome regulatory particle base subunit RPN1
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Glickman M, Rubin D, Fried V, Finley D. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol. 1998;18:3149-62 pubmed
    ..Of the remaining 11 subunits that we have identified (Rpn1 to Rpn3 and Rpn5 to Rpn12), 8 are encoded by previously described genes and 3 are encoded by genes not previously ..
  2. Baranes Bachar K, Baranes Bacher K, Khalaila I, Ivantsiv Y, Lavut A, Voloshin O, et al. New interacting partners of the F-box protein Ufo1 of yeast. Yeast. 2008;25:733-43 pubmed publisher
    ..We show directly that the UIMs are crucial for Ufo1 ubiquitylation in vivo, indicating that they facilitate turnover of SCF Ufo1 complexes. This allows recycling of the core subunits of the SCF complex and cell cycle progression. ..
  3. 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. ..
  4. Park S, Roelofs J, Kim W, Robert J, Schmidt M, Gygi S, et al. Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature. 2009;459:866-70 pubmed publisher
    ..We have also identified an apparent intermediate in base assembly, BP1, which contains Rpn1, three Rpts and Hsm3, a chaperone for base assembly...
  5. 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. ..
  6. 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. ..
  7. Kim I, Mi K, Rao H. Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. Mol Biol Cell. 2004;15:3357-65 pubmed
    ..Furthermore, Ufd2 and the proteasome subunit Rpn1 compete for the binding of Rad23, suggesting that Rad23 forms separate complexes with them...
  8. Barrault M, Richet N, Godard C, Murciano B, Le Tallec B, Rousseau E, et al. Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly. Proc Natl Acad Sci U S A. 2012;109:E1001-10 pubmed publisher
    ..important for normal growth and directly targets the carboxyl-terminal (C-terminal) domain of Rpt1 of the Rpt1-Rpt2-Rpn1 assembly intermediate...
  9. 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. ..

More Information

Publications51

  1. 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. ..
  2. 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
    ..Our data suggest a potential mechanism for this protein-protein stabilization and also suggest that an intact proteasomal regulatory particle is required for responses to DNA damage. ..
  3. Elsasser S, Gali R, Schwickart M, Larsen C, Leggett D, Müller B, et al. Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nat Cell Biol. 2002;4:725-30 pubmed
    ..A component of the base, Rpn1, specifically recognizes the UBL domain of Rad23 through its leucine-rich-repeat-like (LRR-like) domain...
  4. 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. ..
  5. 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. ..
  6. Kaplun L, Tzirkin R, Bakhrat A, Shabek N, Ivantsiv Y, Raveh D. The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease. Mol Cell Biol. 2005;25:5355-62 pubmed
    ..These results establish a role for Ddi1 in the degradation of a natural ubiquitylated substrate. The specific interaction between Ho and Ddi1 identifies an additional function associated with DNA damage involved in its degradation. ..
  7. 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. ..
  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. Effantin G, Rosenzweig R, Glickman M, Steven A. Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2. J Mol Biol. 2009;386:1204-11 pubmed publisher
    b>Rpn1 (109 kDa) and Rpn2 (104 kDa) are components of the 19S regulatory complex of the proteasome...
  10. 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
    ..dock at two different receptor sites embedded within a single subunit of the 19 S proteasome regulatory particle, Rpn1. Their association/dissociation constants and affinities for Rpn1 are similar...
  11. Saeki Y, Sone T, Toh e A, Yokosawa H. Identification of ubiquitin-like protein-binding subunits of the 26S proteasome. Biochem Biophys Res Commun. 2002;296:813-9 pubmed
    ..The base subcomplex of the RP was found to have the ability to bind the Ubl. By cross-linking experiments, Rpn1 and Rpn2 were identified as Ubl-binding subunits...
  12. Rosenzweig R, Osmulski P, Gaczynska M, Glickman M. The central unit within the 19S regulatory particle of the proteasome. Nat Struct Mol Biol. 2008;15:573-80 pubmed publisher
    ..Here we describe a previously unknown functional unit within the 19S, comprising two subunits, Rpn1 and Rpn2. These toroids physically link the site of substrate recruitment with the site of proteolysis...
  13. 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. ..
  14. Finley D, Tanaka K, Mann C, Feldmann H, Hochstrasser M, Vierstra R, et al. Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle. Trends Biochem Sci. 1998;23:244-5 pubmed
  15. Waite K, De La Mota Peynado A, Vontz G, Roelofs J. Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles. J Biol Chem. 2016;291:3239-53 pubmed publisher
    ..Thus, in addition to the well characterized transcriptional up-regulation of genes encoding proteasome subunits, cells are also capable of down-regulating cellular levels of proteasomes through proteaphagy. ..
  16. 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. ..
  17. 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. ..
  18. 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
  19. 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...
  20. Loayza D, Tam A, Schmidt W, Michaelis S. Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae. Mol Biol Cell. 1998;9:2767-84 pubmed
  21. 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. ..
  22. 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
    ..These studies suggest that Rpn11 is stabilized following its incorporation into proteasomes. The instability of Rpn11 and the defects of rpn3 mutants are apparently caused by a failure to recruit Rpn11 into mature proteasomes. ..
  23. Funakoshi M, Sasaki T, Nishimoto T, Kobayashi H. Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A. 2002;99:745-50 pubmed
    ..of the Dsk2p-mediated lethality proved to be temperature-sensitive mutations in two proteasome subunits, rpn1 and pre2. K48-linked ubiquitin-dependent degradation was impaired by disruption of the DSK2 gene...
  24. Park S, Li X, Kim H, Singh C, Tian G, Hoyt M, et al. Reconfiguration of the proteasome during chaperone-mediated assembly. Nature. 2013;497:512-6 pubmed publisher
    ..Thus, the Rpt-CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme. ..
  25. 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
    ..receptors in yeast are collectively nonessential for ubiquitin recognition and identified a sixth receptor, Rpn1. A site ( T1: ) in the Rpn1 toroid recognized ubiquitin and ubiquitin-like ( UBL: ) domains of substrate shuttling ..
  26. Hochstrasser M. Ubiquitin-dependent protein degradation. Annu Rev Genet. 1996;30:405-39 pubmed
    ..This diversity underlies both the high substrate specificity of the ubiquitin system and the variety of regulatory mechanisms that it serves. ..
  27. Bashore C, Dambacher C, Goodall E, Matyskiela M, Lander G, Martin A. Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome. Nat Struct Mol Biol. 2015;22:712-9 pubmed publisher
    ..Ubp6 may thus act as a ubiquitin-dependent 'timer' to coordinate individual processing steps at the proteasome and modulate substrate degradation. ..
  28. Faza M, Kemmler S, Jimeno S, González Aguilera C, Aguilera A, Hurt E, et al. Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery. J Cell Biol. 2009;184:833-46 pubmed publisher
    ..Thus, Sem1 is a versatile protein that might stabilize multiple protein complexes involved in diverse pathways. ..
  29. 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. ..
  30. 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...
  31. Sekiguchi T, Sasaki T, Funakoshi M, Ishii T, Saitoh Y, Kaneko S, et al. Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast. Biochem Biophys Res Commun. 2011;411:555-61 pubmed publisher
    ..These results indicate that ubiquitination in the UBL domain of Dsk2 has in vivo functions in the ubiquitin-proteasome pathway in yeast. ..
  32. Nekrasov V, Smith M, Peak Chew S, Kilmartin J. Interactions between centromere complexes in Saccharomyces cerevisiae. Mol Biol Cell. 2003;14:4931-46 pubmed
    ..These results show an increasingly complex structure for the S. cerevisiae centromere and a probable conservation of structure between parts of the centromeres of S. cerevisiae and S. pombe. ..
  33. Panasenko O, David F, Collart M. Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination. Genetics. 2009;181:447-60 pubmed publisher
    ..Finally, our study demonstrated an interaction of EGD/NAC with the proteasome and revealed the importance of the Not4p E3 ligase, responsible for EGD/NAC ubiquitination, in this association. ..
  34. Wang X, Yen J, Kaiser P, Huang L. Regulation of the 26S proteasome complex during oxidative stress. Sci Signal. 2010;3:ra88 pubmed publisher
  35. 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
    ..The Ddi1-UbL domain binds Rpn1 of the 19S RP, the Ddi1-UbA domain binds ubiquitin chains on the degradation substrate...
  36. 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
    ..Yeast uses UIM in RPN10 and LRR in RPN1. Overall, multiple proteasome subunits are responsible for the direct and/or indirect recognition of ubiquitylated ..
  37. Kim I, Ahn J, Liu C, Tanabe K, Apodaca J, Suzuki T, et al. The Png1-Rad23 complex regulates glycoprotein turnover. J Cell Biol. 2006;172:211-9 pubmed
    ..We propose that the substrate specificity of Rad23 and other Ub binding proteins is determined by their interactions with various cofactors involved in specific degradation pathways. ..
  38. Chen X, Randles L, Shi K, Tarasov S, Aihara H, Walters K. Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome. Structure. 2016;24:1257-1270 pubmed publisher
    Three receptors (Rpn1/S2/PSMD2, Rpn10/S5a, Rpn13/Adrm1) in the proteasome bind substrates by interacting with conjugated ubiquitin chains and/or shuttle factors (Rad23/HR23, Dsk2/PLIC/ubiquilin, Ddi1) that carry ubiquitinated substrates ..
  39. Krutauz D, Reis N, Nakasone M, Siman P, Zhang D, Kirkpatrick D, et al. Extended ubiquitin species are protein-based DUB inhibitors. Nat Chem Biol. 2014;10:664-70 pubmed publisher
  40. 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. ..
  41. 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. ..
  42. Hatanaka A, Chen B, Sun J, Mano Y, Funakoshi M, Kobayashi H, et al. Fub1p, a novel protein isolated by boundary screening, binds the proteasome complex. Genes Genet Syst. 2011;86:305-14 pubmed
    ..Finally, boundary assay showed that human PSMF1 also exhibited boundary establishment activity in yeast. Our results defined the functional correlation between Fub1p and PSMF1. ..