RPN5

Summary

Gene Symbol: RPN5
Description: proteasome regulatory particle lid subunit RPN5
Alias: NAS5, proteasome regulatory particle lid subunit RPN5
Species: Saccharomyces cerevisiae S288c
Products:     RPN5

Top Publications

  1. 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. ..
  2. 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. ..
  3. 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. ..
  4. 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 characterized for ..
  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. 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. Isono E, Saito N, Kamata N, Saeki Y, Toh e A. Functional analysis of Rpn6p, a lid component of the 26 S proteasome, using temperature-sensitive rpn6 mutants of the yeast Saccharomyces cerevisiae. J Biol Chem. 2005;280:6537-47 pubmed
  8. 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. ..
  9. 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
    ..By using nat1, nat3, and mak3 deletion mutants, we found that 8 subunits, Rpt4, Rpt5, Rpt6, Rpn2, Rpn3, Rpn5, Rpn6, and Rpn8, were NatA substrates, and that 2 subunits, Rpt3 and Rpn11, were NatB substrates...

More Information

Publications36

  1. 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. ..
  2. 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. ..
  3. 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. ..
  4. Maytal Kivity V, Pick E, Piran R, Hofmann K, Glickman M. The COP9 signalosome-like complex in S. cerevisiae and links to other PCI complexes. Int J Biochem Cell Biol. 2003;35:706-15 pubmed
    ..Two CSN subunits, Csn9 and Csi1, interact with the proteasome lid subunit Rpn5. Pci8/Csn11 has previously been shown to interact with eIF3...
  5. 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. ..
  6. Stirling P, Chan Y, Minaker S, Aristizabal M, Barrett I, Sipahimalani P, et al. R-loop-mediated genome instability in mRNA cleavage and polyadenylation mutants. Genes Dev. 2012;26:163-75 pubmed publisher
    ..Our findings illuminate how mCP maintains genome integrity by suppressing R-loop formation and suggest that this function may be relevant to certain human cancers. ..
  7. 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. ..
  8. Ben Aroya S, Agmon N, Yuen K, Kwok T, McManus K, Kupiec M, et al. Proteasome nuclear activity affects chromosome stability by controlling the turnover of Mms22, a protein important for DNA repair. PLoS Genet. 2010;6:e1000852 pubmed publisher
    ..Our results demonstrate for the first time that a double strand break repair protein is a proteasome target, and thus link nuclear proteasomal activity and DSB repair. ..
  9. 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. ..
  10. 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. ..
  11. Smith N, Adle D, Zhao M, Qin X, Kim H, Lee J. Endoplasmic Reticulum-associated Degradation of Pca1p, a Polytopic Protein, via Interaction with the Proteasome at the Membrane. J Biol Chem. 2016;291:15082-92 pubmed publisher
    ..These results indicate that extraction and degradation of polytopic membrane proteins at the ER is a coupled event. This mechanism would relieve the cost of exposed hydrophobic domains in the cytosol during ERAD. ..
  12. 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. ..
  13. 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
    ..with the ubiquitin receptor Rpn10, whereas the PCI domain mediates interaction with the neighboring PCI subunit Rpn5. The Rpn9-Rpn5 interface highlights two structural motifs on the winged helix module forming a hydrophobic center ..
  14. 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. ..
  15. 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 ..
  16. 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. ..
  17. 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
    ..5 Ã… resolution, revealing how Rpn11 is inhibited through its interaction with a neighboring lid subunit, Rpn5. Through mutagenesis of specific residues, we describe the network of interactions that are required to stabilize ..
  18. Funakoshi M, Hochstrasser M. Small epitope-linker modules for PCR-based C-terminal tagging in Saccharomyces cerevisiae. Yeast. 2009;26:185-92 pubmed publisher
    ..The set of plasmids has been deposited in the non-profit plasmid repository Addgene (http://www.addgene.org). ..
  19. Sharon M, Taverner T, Ambroggio X, Deshaies R, Robinson C. Structural organization of the 19S proteasome lid: insights from MS of intact complexes. PLoS Biol. 2006;4:e267 pubmed
    ..More generally, the results highlight the potential of mass spectrometry to add crucial insight into the structural organization of an endogenous, wild-type complex. ..
  20. Ha S, Ju D, Xie Y. The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits. Biochem Biophys Res Commun. 2012;419:226-31 pubmed publisher
    ..Using a photo-crosslinking-label transfer method, we captured three 19S RP subunits (Rpt1, Rpn2 and Rpn5) that bind the Ub-independent degron of Rpn4...
  21. 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. ..
  22. 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. ..
  23. Chien C, Chen R. Cdc48 chaperone and adaptor Ubx4 distribute the proteasome in the nucleus for anaphase proteolysis. J Biol Chem. 2013;288:37180-91 pubmed publisher
    ..Our data propose that Cdc48-Ubx4 acts on the proteasome and uses the chaperone activity to promote its nuclear distribution, thereby optimizing the proteasome level for efficient degradation of mitotic regulators...
  24. 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
  25. 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. ..
  26. 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. ..
  27. Marshall R, McLoughlin F, Vierstra R. Autophagic Turnover of Inactive 26S Proteasomes in Yeast Is Directed by the Ubiquitin Receptor Cue5 and the Hsp42 Chaperone. Cell Rep. 2016;16:1717-1732 pubmed publisher
    ..Together, Cue5 and Hsp42 provide a quality control checkpoint in yeast directed at recycling dysfunctional 26S proteasomes. ..