| Structural highlights
Function
[RPN1_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.[1] [RPN7_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). [RPN12_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Necessary for activation of the CDC28 kinase. [RPN2_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.[2] [RPN5_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.[3] [RPN8_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.[4] [RPN11_YEAST] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.[5] [RPN3_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [RPN10_YEAST] Multiubiquitin binding protein. [RPN13_YEAST] Component of the 19S cap proteasome complex which acts as a regulatory subunit of the 26S proteasome, involved in the ATP-dependent degradation of ubiquitinated proteins.[6] [7] [RPN9_YEAST] Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [RPN6_YEAST] Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, RPN6 is required for proteasome assembly.[8] [9] [10] [SEM1_YEAST] Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.[11] [12]
Publication Abstract from PubMed
In eukaryotic cells, the ubiquitin-proteasome system (UPS) is responsible for the regulated degradation of intracellular proteins. The 26S holocomplex comprises the core particle (CP), where proteolysis takes place, and one or two regulatory particles (RPs). The base of the RP is formed by a heterohexameric AAA+ ATPase module, which unfolds and translocates substrates into the CP. Applying single-particle cryo-electron microscopy (cryo-EM) and image classification to samples in the presence of different nucleotides and nucleotide analogs, we were able to observe four distinct conformational states (s1 to s4). The resolution of the four conformers allowed for the construction of atomic models of the AAA+ ATPase module as it progresses through the functional cycle. In a hitherto unobserved state (s4), the gate controlling access to the CP is open. The structures described in this study allow us to put forward a model for the 26S functional cycle driven by ATP hydrolysis.
Structural insights into the functional cycle of the ATPase module of the 26S proteasome.,Wehmer M, Rudack T, Beck F, Aufderheide A, Pfeifer G, Plitzko JM, Forster F, Schulten K, Baumeister W, Sakata E Proc Natl Acad Sci U S A. 2017 Feb 7;114(6):1305-1310. doi:, 10.1073/pnas.1621129114. Epub 2017 Jan 23. PMID:28115689[13]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Glickman MH, Rubin DM, Fried VA, Finley D. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol. 1998 Jun;18(6):3149-62. PMID:9584156
- ↑ Glickman MH, Rubin DM, Fried VA, Finley D. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol. 1998 Jun;18(6):3149-62. PMID:9584156
- ↑ Saito A, Watanabe TK, Shimada Y, Fujiwara T, Slaughter CA, DeMartino GN, Tanahashi N, Tanaka K. cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome. Gene. 1997 Dec 12;203(2):241-50. PMID:9426256
- ↑ Glickman MH, Rubin DM, Fried VA, Finley D. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol. 1998 Jun;18(6):3149-62. PMID:9584156
- ↑ Chen L, Romero L, Chuang SM, Tournier V, Joshi KK, Lee JA, Kovvali G, Madura K. Sts1 plays a key role in targeting proteasomes to the nucleus. J Biol Chem. 2011 Jan 28;286(4):3104-18. doi: 10.1074/jbc.M110.135863. Epub 2010 , Nov 12. PMID:21075847 doi:10.1074/jbc.M110.135863
- ↑ Fischer M, Hilt W, Richter-Ruoff B, Gonen H, Ciechanover A, Wolf DH. The 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett. 1994 Nov 21;355(1):69-75. PMID:7957966
- ↑ Verma R, Chen S, Feldman R, Schieltz D, Yates J, Dohmen J, Deshaies RJ. Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol Biol Cell. 2000 Oct;11(10):3425-39. PMID:11029046
- ↑ Saito A, Watanabe TK, Shimada Y, Fujiwara T, Slaughter CA, DeMartino GN, Tanahashi N, Tanaka K. cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome. Gene. 1997 Dec 12;203(2):241-50. PMID:9426256
- ↑ Santamaria PG, Finley D, Ballesta JP, Remacha M. Rpn6p, a proteasome subunit from Saccharomyces cerevisiae, is essential for the assembly and activity of the 26 S proteasome. J Biol Chem. 2003 Feb 28;278(9):6687-95. Epub 2002 Dec 16. PMID:12486135 doi:10.1074/jbc.M209420200
- ↑ 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 Feb 25;280(8):6537-47. Epub 2004 Dec 15. PMID:15611133 doi:10.1074/jbc.M409364200
- ↑ Faza MB, Kemmler S, Jimeno S, Gonzalez-Aguilera C, Aguilera A, Hurt E, Panse VG. Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery. J Cell Biol. 2009 Mar 23;184(6):833-46. doi: 10.1083/jcb.200810059. Epub 2009 Mar, 16. PMID:19289793 doi:http://dx.doi.org/10.1083/jcb.200810059
- ↑ 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 Jul 2;279(27):28807-16. Epub 2004 Apr 26. PMID:15117943 doi:http://dx.doi.org/10.1074/jbc.M403165200
- ↑ Wehmer M, Rudack T, Beck F, Aufderheide A, Pfeifer G, Plitzko JM, Forster F, Schulten K, Baumeister W, Sakata E. Structural insights into the functional cycle of the ATPase module of the 26S proteasome. Proc Natl Acad Sci U S A. 2017 Feb 7;114(6):1305-1310. doi:, 10.1073/pnas.1621129114. Epub 2017 Jan 23. PMID:28115689 doi:http://dx.doi.org/10.1073/pnas.1621129114
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