| Rpn10, but not ubiquitylated-Rpn10, binds Rpn9 in vitro: ubiquitylation functions to dissociate modified ubiquitin receptors from their targets, a function that promotes cyclic activity of ubiquitin receptors | Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism.
Keren-Kaplan T, Zeev Peters L, Levin-Kravets O, Attali I, Kleifeld O, Shohat N, Artzi S, Zucker O, Pilzer I, Reis N, Glickman MH, Ben-Aroya S, Prag G., Free PMC Article | 10/6/2018 |
| Genetic, bioinformatics, biochemical and biophysical data show that attraction between this alpha1-conjugated ubiquitin and the HECT ubiquitin-binding patch pulls the alpha1-helix out of the interface, thereby promoting trimerization. Strikingly, trimerization renders the ubiquitin ligase inactive. | Ubiquitylation-dependent oligomerization regulates activity of Nedd4 ligases.
Attali I, Tobelaim WS, Persaud A, Motamedchaboki K, Simpson-Lavy KJ, Mashahreh B, Levin-Kravets O, Keren-Kaplan T, Pilzer I, Kupiec M, Wiener R, Wolf DA, Rotin D, Prag G., Free PMC Article | 07/15/2017 |
| functional yeast proteasomes have the capacity to associate and dissociate with Rpn10 and that Rpn10 monoubiquitination decreases the Rpn10-proteasome and Rpn10-Dsk2 associations. | Rpn10 monoubiquitination orchestrates the association of the ubiquilin-type DSK2 receptor with the proteasome.
Zuin A, Bichmann A, Isasa M, Puig-Sàrries P, Díaz LM, Crosas B. | 03/19/2016 |
| Mutations in this disordered region promote ubiquitin chain extension of Rpn10. | An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination.
Puig-Sàrries P, Bijlmakers MJ, Zuin A, Bichmann A, Pons M, Crosas B. | 11/14/2015 |
| X-ray analysis revealed that these crystals of Rpn10 belonged to the monoclinic system C2, with unit-cell parameters a = 107.3, b = 49.7, c = 81.3 A, alpha = gamma = 90.0, beta = 130.5 degrees | Purification and crystallization of mono-ubiquitylated ubiquitin receptor Rpn10.
Keren-Kaplan T, Prag G., Free PMC Article | 11/24/2012 |
| On the basis of the mutual positions of Rpn10 and Rpn13, we propose a model for polyubiquitin binding to the 26S proteasome | Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy.
Sakata E, Bohn S, Mihalache O, Kiss P, Beck F, Nagy I, Nickell S, Tanaka K, Saeki Y, Förster F, Baumeister W., Free PMC Article | 03/31/2012 |
| It is conceivable that Rpn10/Rpn11 interaction couples proteasome assembly to substrate binding. | Synthetic lethality of rpn11-1 rpn10Δ is linked to altered proteasome assembly and activity.
Chandra A, Chen L, Madura K., Free PMC Article | 02/26/2011 |
| Data report that Rpn10 is monoubiquitinated in vivo and that this modification has profound effects on proteasome function. | Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome.
Isasa M, Katz EJ, Kim W, Yugo V, González S, Kirkpatrick DS, Thomson TM, Finley D, Gygi SP, Crosas B., Free PMC Article | 07/5/2010 |
| Data describe formation of ternary complexes of Dsk2 and Rpn10 with (poly)ubiquitin and found that, depending on the ubiquitin chain length, the orientation of the resulting complex is entirely different, providing for alternate signals. | Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
Zhang D, Chen T, Ziv I, Rosenzweig R, Matiuhin Y, Bronner V, Glickman MH, Fushman D., Free PMC Article | 02/8/2010 |
| The yeast homologue of S5a, Rpn10, enhanced the proteasomal degradation of troponin I to the same extent as S5a. | S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains.
Kim HT, Kim KP, Uchiki T, Gygi SP, Goldberg AL., Free PMC Article | 01/21/2010 |
| Mutations in the hydrophobic core of ubiquitin affect its recognition by RPN10. | Mutations in the hydrophobic core of ubiquitin differentially affect its recognition by receptor proteins.
Haririnia A, Verma R, Purohit N, Twarog MZ, Deshaies RJ, Bolon D, Fushman D., Free PMC Article | 01/21/2010 |
| These findings underscore a broad role for Rpn10 in turnover of ubiquitylated substrates but a relatively modest role for its ubiquitin-binding UIM domain. | Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway.
Mayor T, Graumann J, Bryan J, MacCoss MJ, Deshaies RJ. | 01/21/2010 |
| These results suggest that Rpn10p is the receptor that binds the polyubiquitin chain during ubiquitin-dependent proteolysis of Gcn4p. | Rpn10p is a receptor for ubiquitinated Gcn4p in proteasomal proteolysis.
Seong KM, Baek JH, Ahn BY, Yu MH, Kim J. | 01/21/2010 |