The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle - PubMed (original) (raw)
The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle
Eri Sakata et al. Mol Cell. 2011.
Free article
Abstract
The 26S proteasome is a 2.5 MDa macromolecular machine responsible for targeted protein degradation. Recently, four chaperones were identified that promote the assembly of the 19S regulatory particle (RP). Here, we probe the dynamic architecture of the proteasome by applying quantitative proteomics and mass spectrometry (MS) of intact complexes to provide a detailed characterization of how Ubp6 assists this assembly process. Our MS data demonstrate stoichiometric binding of chaperones and Ubp6 to the basal part of the RP. Genetic interactions of Ubp6 with Hsm3, but not with the other chaperones, indicate a functional overlay with Hsm3. Our biochemical data identified Ubp6 as an additional member of the Hsm3 module. Deletions of ubp6 with hsm3 perturb 26S proteasome assembly, which we attribute to an accumulation of ubiquitylated substrates on these assembly precursors. We therefore propose that Ubp6 facilitates proteasomal assembly by clearing ubiquitylated substrates from assembly precursors by its deubiquitylating activity.
Copyright © 2011 Elsevier Inc. All rights reserved.
Similar articles
- Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome.
Le Tallec B, Barrault MB, Guérois R, Carré T, Peyroche A. Le Tallec B, et al. Mol Cell. 2009 Feb 13;33(3):389-99. doi: 10.1016/j.molcel.2009.01.010. Mol Cell. 2009. PMID: 19217412 - Structural characterization of the interaction of Ubp6 with the 26S proteasome.
Aufderheide A, Beck F, Stengel F, Hartwig M, Schweitzer A, Pfeifer G, Goldberg AL, Sakata E, Baumeister W, Förster F. Aufderheide A, et al. Proc Natl Acad Sci U S A. 2015 Jul 14;112(28):8626-31. doi: 10.1073/pnas.1510449112. Epub 2015 Jun 30. Proc Natl Acad Sci U S A. 2015. PMID: 26130806 Free PMC article. - Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome.
Bashore C, Dambacher CM, Goodall EA, Matyskiela ME, Lander GC, Martin A. Bashore C, et al. Nat Struct Mol Biol. 2015 Sep;22(9):712-9. doi: 10.1038/nsmb.3075. Epub 2015 Aug 24. Nat Struct Mol Biol. 2015. PMID: 26301997 Free PMC article. - Assembly and function of the proteasome.
Saeki Y, Tanaka K. Saeki Y, et al. Methods Mol Biol. 2012;832:315-37. doi: 10.1007/978-1-61779-474-2_22. Methods Mol Biol. 2012. PMID: 22350895 Review. - Proteomics of proteasome complexes and ubiquitinated proteins.
Wang X, Guerrero C, Kaiser P, Huang L. Wang X, et al. Expert Rev Proteomics. 2007 Oct;4(5):649-65. doi: 10.1586/14789450.4.5.649. Expert Rev Proteomics. 2007. PMID: 17941820 Review.
Cited by
- Protein-protein interactions: switch from classical methods to proteomics and bioinformatics-based approaches.
Ngounou Wetie AG, Sokolowska I, Woods AG, Roy U, Deinhardt K, Darie CC. Ngounou Wetie AG, et al. Cell Mol Life Sci. 2014 Jan;71(2):205-28. doi: 10.1007/s00018-013-1333-1. Epub 2013 Apr 12. Cell Mol Life Sci. 2014. PMID: 23579629 Free PMC article. Review. - The prolific ATL family of RING-H2 ubiquitin ligases.
Guzmán P. Guzmán P. Plant Signal Behav. 2012 Aug;7(8):1014-21. doi: 10.4161/psb.20851. Epub 2012 Jul 25. Plant Signal Behav. 2012. PMID: 22827943 Free PMC article. Review. - Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly.
Barrault MB, Richet N, Godard C, Murciano B, Le Tallec B, Rousseau E, Legrand P, Charbonnier JB, Le Du MH, Guérois R, Ochsenbein F, Peyroche A. Barrault MB, et al. Proc Natl Acad Sci U S A. 2012 Apr 24;109(17):E1001-10. doi: 10.1073/pnas.1116538109. Epub 2012 Mar 29. Proc Natl Acad Sci U S A. 2012. PMID: 22460800 Free PMC article. - A mass spectrometry-based hybrid method for structural modeling of protein complexes.
Politis A, Stengel F, Hall Z, Hernández H, Leitner A, Walzthoeni T, Robinson CV, Aebersold R. Politis A, et al. Nat Methods. 2014 Apr;11(4):403-406. doi: 10.1038/nmeth.2841. Epub 2014 Feb 9. Nat Methods. 2014. PMID: 24509631 Free PMC article. - Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation.
Śledź P, Unverdorben P, Beck F, Pfeifer G, Schweitzer A, Förster F, Baumeister W. Śledź P, et al. Proc Natl Acad Sci U S A. 2013 Apr 30;110(18):7264-9. doi: 10.1073/pnas.1305782110. Epub 2013 Apr 15. Proc Natl Acad Sci U S A. 2013. PMID: 23589842 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases