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Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle.

Lu Y, Wu J, Dong Y, Chen S, Sun S, Ma YB, Ouyang Q, Finley D, Kirschner MW, Mao Y
Mol Cell 67 322-333.e6 (2017)
Related entries: 5vgz, 5vhf, 5vhh, 5vhi, 5vhj, 5vhm, 5vhn, 5vho, 5vhp, 5vhq, 5vhs

Cited: 23 times
EuropePMC logo PMID: 28689658

Abstract

The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 Å resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions. Remarkably, the p28-bound AAA ring does not form a channel in the free RP and spontaneously samples multiple "open" and "closed" topologies at the Rpt2-Rpt6 and Rpt3-Rpt4 interfaces. Our analysis suggests that p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for RP engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly.

Articles - 5vhr mentioned but not cited (1)

  1. Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle. Lu Y, Wu J, Dong Y, Chen S, Sun S, Ma YB, Ouyang Q, Finley D, Kirschner MW, Mao Y. Mol Cell 67 322-333.e6 (2017)


Reviews citing this publication (7)

  1. Cryo-EM for Small Molecules Discovery, Design, Understanding, and Application. Scapin G, Potter CS, Carragher B. Cell Chem Biol 25 1318-1325 (2018)
  2. AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms. Zhang S, Mao Y. Biomolecules 10 E629 (2020)
  3. A Potential Mechanism for Targeting Aggregates With Proteasomes and Disaggregases in Liquid Droplets. Mee Hayes E, Sirvio L, Ye Y. Front Aging Neurosci 14 854380 (2022)
  4. Adaptation of Proteasomes and Lysosomes to Cellular Environments. Mebratu YA, Negasi ZH, Dutta S, Rojas-Quintero J, Tesfaigzi Y. Cells 9 E2221 (2020)
  5. The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors. Creekmore BC, Chang YW, Lee EB. J Neuropathol Exp Neurol 80 494-513 (2021)
  6. Reversible protein assemblies in the proteostasis network in health and disease. Kohler V, Andréasson C. Front Mol Biosci 10 1155521 (2023)
  7. Wiggle and Shake: Managing and Exploiting Conformational Dynamics during Proteasome Biogenesis. Betancourt D, Lawal T, Tomko RJ. Biomolecules 13 1223 (2023)

Articles citing this publication (15)

  1. Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome. Dong Y, Zhang S, Wu Z, Li X, Wang WL, Zhu Y, Stoilova-McPhie S, Lu Y, Finley D, Mao Y. Nature 565 49-55 (2019)
  2. Massively parallel unsupervised single-particle cryo-EM data clustering via statistical manifold learning. Wu J, Ma YB, Congdon C, Brett B, Chen S, Xu Y, Ouyang Q, Mao Y. PLoS One 12 e0182130 (2017)
  3. Proline- and Arginine-Rich Peptides as Flexible Allosteric Modulators of Human Proteasome Activity. Giżyńska M, Witkowska J, Karpowicz P, Rostankowski R, Chocron ES, Pickering AM, Osmulski P, Gaczynska M, Jankowska E. J Med Chem 62 359-370 (2019)
  4. Reversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function. Liu X, Xiao W, Zhang Y, Wiley SE, Zuo T, Zheng Y, Chen N, Chen L, Wang X, Zheng Y, Huang L, Lin S, Murphy AN, Dixon JE, Xu P, Guo X. Proc Natl Acad Sci U S A 117 328-336 (2020)
  5. An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes. Nemec AA, Peterson AK, Warnock JL, Reed RG, Tomko RJ. Cell Rep 26 483-495.e5 (2019)
  6. Ubiquitin-dependent switch during assembly of the proteasomal ATPases mediated by Not4 ubiquitin ligase. Fu X, Sokolova V, Webb KJ, Old W, Park S. Proc Natl Acad Sci U S A 115 13246-13251 (2018)
  7. What Will Computational Modeling Approaches Have to Say in the Era of Atomistic Cryo-EM Data? Fraser JS, Lindorff-Larsen K, Bonomi M. J Chem Inf Model 60 2410-2412 (2020)
  8. An empirical energy landscape reveals mechanism of proteasome in polypeptide translocation. Fang R, Hon J, Zhou M, Lu Y. Elife 11 e71911 (2022)
  9. Genetically incorporated crosslinkers reveal NleE attenuates host autophagy dependent on PSMD10. Li J, Guo S, Chai F, Sun Q, Li P, Gao L, Dai L, Ouyang X, Zhou Z, Zhou L, Cheng W, Qi S, Lu K, Ren H. Elife 10 e69047 (2021)
  10. Kinectin1 depletion promotes EGFR degradation via the ubiquitin-proteosome system in cutaneous squamous cell carcinoma. Ma J, Ma S, Zhang Y, Shen Y, Huang L, Lu T, Wang L, Wen Y, Ding Z. Cell Death Dis 12 995 (2021)
  11. Visualizing Conformational Space of Functional Biomolecular Complexes by Deep Manifold Learning. Wu Z, Chen E, Zhang S, Ma Y, Mao Y. Int J Mol Sci 23 8872 (2022)
  12. Assembly checkpoint of the proteasome regulatory particle is activated by coordinated actions of proteasomal ATPase chaperones. Nahar A, Sokolova V, Sekaran S, Orth JD, Park S. Cell Rep 39 110918 (2022)
  13. Gankyrin modulated non-small cell lung cancer progression via glycolysis metabolism in a YAP1-dependent manner. Yu T, Liu Y, Xue J, Sun X, Zhu D, Ma L, Guo Y, Jin T, Cao H, Chen Y, Zhu T, Li X, Liang H, Du Z, Shan H. Cell Death Discov 8 312 (2022)
  14. Robustness of signal detection in cryo-electron microscopy via a bi-objective-function approach. Wang WL, Yu Z, Castillo-Menendez LR, Sodroski J, Mao Y. BMC Bioinformatics 20 169 (2019)
  15. The penultimate step of proteasomal ATPase assembly is mediated by a switch dependent on the chaperone Nas2. Sekaran S, Park S. J Biol Chem 299 102870 (2023)


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