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Gene Review

RPN10  -  proteasome regulatory particle base...

Saccharomyces cerevisiae S288c

Synonyms: 26S proteasome regulatory subunit RPN10, MCB1, SUN1, YHR200W
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High impact information on RPN10

  • In vivo analyses confirmed that Rad23 and the multiubiquitin binding domain of Rpn10 contribute to Sic1 degradation [1].
  • A single residue in the vWA domain of Rpn10 is essential for amino acid analog resistance, for degrading a ubiquitin fusion degradation substrate and for stabilizing lid-base association [2].
  • It is unclear how a targeted substrate is delivered to the 26S proteasome, inasmuch as Rpn10p, the only known proteasomal subunit that binds multi-Ub chains, has been found to be not essential for degradation of many proteins in the yeast Saccharomyces cerevisiae [3].
  • Importantly, we find that the luminal C-terminal domain of SUN1 interacts with the mammalian ANC-1 homologs nesprins 1 and 2 via their conserved KASH domain [4].
  • We demonstrate that SUN1 is an integral membrane protein located at the inner nuclear membrane [4].

Biological context of RPN10

  • To distinguish whether RPN10 is involved in the turnover of only a small set of cell cycle regulators that includes Sic1 or plays a more general role in the UPS, we sought to develop a general method that would allow us to survey the spectrum of ubiquitylated proteins that selectively accumulate in rpn10Delta cells [5].
  • Because the suppression of a rad23 Delta rpn10 Delta mutant phenotype required both UbL(R23) and UBA domains, our findings support the hypothesis that Rad23 encodes a novel regulatory factor that translocates ubiquitinated substrates to the proteasome [6].
  • Rad23 plays an overlapping role with Rpn10, a proteasome-associated multi-Ub chain binding protein [6].
  • We have carried out genome array profiles from cells with decreased Rpn10/S5a levels using RNAi or from cells treated with proteasome inhibitor MG132 and have thereby identified candidate genes that are regulated as part of a metazoan proteasome network [7].
  • When Rpn10 was deficient in trypanosomes, a 19 S complex without Rpn10 was still formed, whereas cell growth was arrested [8].

Associations of RPN10 with chemical compounds

  • Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain [9].

Physical interactions of RPN10

  • However, studies on RPN10-deleted mutants in yeasts have suggested the presence of other multiubiquitin chain-binding factors functioning in ubiquitin-dependent proteolysis [10].

Other interactions of RPN10

  • A block substitution in the chain-binding ubiquitin interacting motif of RPN10 when combined with a null mutation in RAD23 results in a synthetic defect in protein degradation consistent with the view that the direct and indirect recognition modes function to some extent redundantly in vivo [11].
  • Rpn10, a subunit of the 26S proteasome, has been proposed to act as a receptor for multiubiquitin chains in ubiquitin-dependent proteolysis [10].
  • These results indicate that Rpn9 is needed for incorporating Rpn10 into the 26S proteasome and that Rpn9 participates in the assembly and/or stability of the 26S proteasome [12].
  • The polyubiquitin receptor Rpn10 targets ubiquitylated Sic1 to the 26S proteasome for degradation [5].
  • The resultant precipitate contained Nin1p, Sun1p, TBP1, and the 20S proteasome [13].

Analytical, diagnostic and therapeutic context of RPN10

  • Sequence analyses revealed that these clones encode the S5a/Rpn10 multiubiquitin-binding protein which is a component of the regulatory 19S subunit of the 26S proteasome [14].
  • To determine whether such alternative splicing mechanisms occur in other species, we searched for Rpn10 isoforms in databases and in our original PCR products [15].


  1. Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Verma, R., Oania, R., Graumann, J., Deshaies, R.J. Cell (2004) [Pubmed]
  2. Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome. Fu, H., Reis, N., Lee, Y., Glickman, M.H., Vierstra, R.D. EMBO J. (2001) [Pubmed]
  3. Physical association of ubiquitin ligases and the 26S proteasome. Xie, Y., Varshavsky, A. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  4. SUN1 Interacts with Nuclear Lamin A and Cytoplasmic Nesprins To Provide a Physical Connection between the Nuclear Lamina and the Cytoskeleton. Haque, F., Lloyd, D.J., Smallwood, D.T., Dent, C.L., Shanahan, C.M., Fry, A.M., Trembath, R.C., Shackleton, S. Mol. Cell. Biol. (2006) [Pubmed]
  5. Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets. Mayor, T., Lipford, J.R., Graumann, J., Smith, G.T., Deshaies, R.J. Mol. Cell Proteomics (2005) [Pubmed]
  6. Rad23 promotes the targeting of proteolytic substrates to the proteasome. Chen, L., Madura, K. Mol. Cell. Biol. (2002) [Pubmed]
  7. Identification and characterization of a Drosophila proteasome regulatory network. Lundgren, J., Masson, P., Mirzaei, Z., Young, P. Mol. Cell. Biol. (2005) [Pubmed]
  8. Functional characterization of the 11 non-ATPase subunit proteins in the trypanosome 19 S proteasomal regulatory complex. Li, Z., Wang, C.C. J. Biol. Chem. (2002) [Pubmed]
  9. Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain. Sakata, E., Yamaguchi, Y., Kurimoto, E., Kikuchi, J., Yokoyama, S., Yamada, S., Kawahara, H., Yokosawa, H., Hattori, N., Mizuno, Y., Tanaka, K., Kato, K. EMBO Rep. (2003) [Pubmed]
  10. Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Saeki, Y., Saitoh, A., Toh-e, A., Yokosawa, H. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  11. 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) [Pubmed]
  12. Rpn9 is required for efficient assembly of the yeast 26S proteasome. Takeuchi, J., Fujimuro, M., Yokosawa, H., Tanaka, K., Toh-e, A. Mol. Cell. Biol. (1999) [Pubmed]
  13. Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae. Fujimuro, M., Tanaka, K., Yokosawa, H., Toh-e, A. FEBS Lett. (1998) [Pubmed]
  14. Interaction of the proteasome S5a/Rpn10 multiubiquitin-binding protein and the 8 kDa calcium-binding protein of Schistosoma mansoni. Ram, D., Ziv, E., Lantner, F., Schechter, I. Parasitology (2003) [Pubmed]
  15. The 26S proteasome Rpn10 gene encoding splicing isoforms: evolutional conservation of the genomic organization in vertebrates. Kikukawa, Y., Shimada, M., Suzuki, N., Tanaka, K., Yokosawa, H., Kawahara, H. Biol. Chem. (2002) [Pubmed]
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