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Journal articles on the topic '19S regulatory particle'

Author: Grafiati

Published: 15 June 2024

Last updated: 31 July 2025

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1

Ehlinger, Aaron, and Kylie J. Walters. "Structural Insights into Proteasome Activation by the 19S Regulatory Particle." Biochemistry 52, no. 21 (2013): 3618–28. http://dx.doi.org/10.1021/bi400417a.

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Lim, Hyun-Suk, Chase T. Archer, and Thomas Kodadek. "Identification of a Peptoid Inhibitor of the Proteasome 19S Regulatory Particle." Journal of the American Chemical Society 129, no. 25 (2007): 7750–51. http://dx.doi.org/10.1021/ja072027p.

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3

Rosenzweig, Rina, Pawel A. Osmulski, Maria Gaczynska, and Michael H. Glickman. "The central unit within the 19S regulatory particle of the proteasome." Nature Structural & Molecular Biology 15, no. 6 (2008): 573–80. http://dx.doi.org/10.1038/nsmb.1427.

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Greer, Susanna, Nagini Maganti, Meghna Thakkar, and Agnieszka Truax. "19S ATPase subunits of the 26S proteasome play critical roles in transcription elongation. (167.7)." Journal of Immunology 188, no. 1_Supplement (2012): 167.7. http://dx.doi.org/10.4049/jimmunol.188.supp.167.7.

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Abstract Major histocompatibility class II molecules are cell surface glycoproteins that present extracellular peptides to CD4+ T cells and initiate adaptive immune responses. MHC II molecules are inducibly expressed in response to interferon gamma and are tightly regulated at the level of transcription by a master regulator, the class II transactivator, CIITA. We have recently shown that the 26S proteasome, itself a master regulator of proteins, regulates transcription initiation at interferon gamma inducible CIITApIV and MHC II genes in a degradation independent manner. The 26S proteasome co

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Mendes, Marta L., and Gunnar Dittmar. "Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry." Biomolecules 11, no. 4 (2021): 505. http://dx.doi.org/10.3390/biom11040505.

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The 26S proteasome is a macromolecular complex that degrades proteins maintaining cell homeostasis; thus, determining its structure is a priority to understand its function. Although the 20S proteasome’s structure has been known for some years, the highly dynamic nature of the 19S regulatory particle has presented a challenge to structural biologists. Advances in cryo-electron microscopy (cryo-EM) made it possible to determine the structure of the 19S regulatory particle and showed at least seven different conformational states of the proteasome. However, there are still many questions to be a

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6

Isono, Erika, Kiyoshi Nishihara, Yasushi Saeki, et al. "The Assembly Pathway of the 19S Regulatory Particle of the Yeast 26S Proteasome." Molecular Biology of the Cell 18, no. 2 (2007): 569–80. http://dx.doi.org/10.1091/mbc.e06-07-0635.

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The 26S proteasome consists of the 20S proteasome (core particle) and the 19S regulatory particle made of the base and lid substructures, and it is mainly localized in the nucleus in yeast. To examine how and where this huge enzyme complex is assembled, we performed biochemical and microscopic characterization of proteasomes produced in two lid mutants, rpn5-1 and rpn7-3, and a base mutant ΔN rpn2, of the yeast Saccharomyces cerevisiae. We found that, although lid formation was abolished in rpn5-1 mutant cells at the restrictive temperature, an apparently intact base was produced and localized

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7

Shibahara, Tadashi, Hiroshi Kawasaki, and Hisashi Hirano. "Identification of the 19S regulatory particle subunits from the rice 26S proteasome." European Journal of Biochemistry 269, no. 5 (2002): 1474–83. http://dx.doi.org/10.1046/j.1432-1033.2002.02792.x.

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8

Stanhill, Ariel, Cole M. Haynes, Yuhong Zhang, et al. "An Arsenite-Inducible 19S Regulatory Particle-Associated Protein Adapts Proteasomes to Proteotoxicity." Molecular Cell 23, no. 6 (2006): 875–85. http://dx.doi.org/10.1016/j.molcel.2006.07.023.

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9

Oliveri, Franziska, Steffen Johannes Keller, Heike Goebel, Gerardo Omar Alvarez Salinas, and Michael Basler. "The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo." Life Science Alliance 6, no. 6 (2023): e202201760. http://dx.doi.org/10.26508/lsa.202201760.

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Ubiquitin-independent protein degradation via the 20S proteasome without the 19S regulatory particle has gained increasing attention over the last years. The degradation of the ubiquitin-like modifier FAT10 by the 20S proteasome was investigated in this study. We found that FAT10 was rapidly degraded by purified 20S proteasomes in vitro, which was attributed to the weak folding of FAT10 and the N-terminally disordered tail. To confirm our results in cellulo, we established an inducible RNA interference system in which the AAA-ATPase Rpt2 of the 19S regulatory particle is knocked down to impair

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10

Brockmann, Florian, Nicola Catone, Christine Wünsch, et al. "FAT10 and NUB1L cooperate to activate the 26S proteasome." Life Science Alliance 6, no. 8 (2023): e202201463. http://dx.doi.org/10.26508/lsa.202201463.

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The interaction of the 19S regulatory particle of the 26S proteasome with ubiquitylated proteins leads to gate opening of the 20S core particle and increases its proteolytic activity by binding of the ubiquitin chain to the inhibitory deubiquitylation enzyme USP14 on the 19S regulatory subunit RPN1. Covalent modification of proteins with the cytokine inducible ubiquitin-like modifier FAT10 is an alternative signal for proteasomal degradation. Here, we report that FAT10 and its interaction partner NUB1L facilitate the gate opening of the 20S proteasome in an ubiquitin- and USP14-independent man

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Kimura, Yayoi, Yasushi Saeki, Hideyoshi Yokosawa, Bogdan Polevoda, Fred Sherman, and Hisashi Hirano. "N-Terminal modifications of the 19S regulatory particle subunits of the yeast proteasome." Archives of Biochemistry and Biophysics 409, no. 2 (2003): 341–48. http://dx.doi.org/10.1016/s0003-9861(02)00639-2.

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12

Saeki, Yasushi, Akio Toh-e, Tai Kudo, Hitomi Kawamura, and Keiji Tanaka. "Multiple Proteasome-Interacting Proteins Assist the Assembly of the Yeast 19S Regulatory Particle." Cell 137, no. 5 (2009): 900–913. http://dx.doi.org/10.1016/j.cell.2009.05.005.

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13

Zhang, Xiaonan, Stig Linder, and Martina Bazzaro. "Drug Development Targeting the Ubiquitin–Proteasome System (UPS) for the Treatment of Human Cancers." Cancers 12, no. 4 (2020): 902. http://dx.doi.org/10.3390/cancers12040902.

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Cancer cells are characterized by a higher rate of protein turnover and greater demand for protein homeostasis compared to normal cells. In this scenario, the ubiquitin–proteasome system (UPS), which is responsible for the degradation of over 80% of cellular proteins within mammalian cells, becomes vital to cancer cells, making the UPS a critical target for the discovery of novel cancer therapeutics. This review systematically categorizes all current reported small molecule inhibitors of the various essential components of the UPS, including ubiquitin-activating enzymes (E1s), ubiquitin-conjug

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14

Bailly, Eric, and Steven I. Reed. "Functional Characterization of Rpn3 Uncovers a Distinct 19S Proteasomal Subunit Requirement for Ubiquitin-Dependent Proteolysis of Cell Cycle Regulatory Proteins in Budding Yeast." Molecular and Cellular Biology 19, no. 10 (1999): 6872–90. http://dx.doi.org/10.1128/mcb.19.10.6872.

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ABSTRACT By selectively eliminating ubiquitin-conjugated proteins, the 26S proteasome plays a pivotal role in a large variety of cellular regulatory processes, particularly in the control of cell cycle transitions. Access of ubiquitinated substrates to the inner catalytic chamber within the 20S core particle is mediated by the 19S regulatory particle (RP), whose subunit composition in budding yeast has been recently elucidated. In this study, we have investigated the cell cycle defects resulting from conditional inactivation of one of these RP components, the essential non-ATPase Rpn3/Sun2 sub

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Peng, Zhaohua, Jeffrey M. Staub, Giovanna Serino, et al. "The Cellular Level of PR500, a Protein Complex Related to the 19S Regulatory Particle of the Proteasome, Is Regulated in Response to Stresses in Plants." Molecular Biology of the Cell 12, no. 2 (2001): 383–92. http://dx.doi.org/10.1091/mbc.12.2.383.

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In Arabidopsis seedlings and cauliflower florets, Rpn6 (a proteasome non-ATPase regulatory subunit) was found in two distinct protein complexes of ∼800 and 500 kDa, respectively. The large complex likely represents the proteasome 19S regulator particle (RP) because it displays the expected subunit composition and all characteristics. The small complex, designated PR500, shares at least three subunits with the “lid” subcomplex of 19S RP and is loosely associated with an hsp70 protein. In ArabidopsisCOP9 signalosome mutants, PR500 was specifically absent or reduced to an extent that correlates w

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16

Rosenzweig, Rina, and Michael H. Glickman. "Chaperone-driven proteasome assembly." Biochemical Society Transactions 36, no. 5 (2008): 807–12. http://dx.doi.org/10.1042/bst0360807.

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Assembly of the 34-subunit, 2.5 MDa 26S proteasome is a carefully choreographed intricate process. It starts with formation of a seven-membered α-ring that serves as a template for assembly of the complementary β-ring-forming ‘half-proteasomes’. Dimerization results in a latent 20S core particle that can serve further as a platform for 19S regulatory particle attachment and formation of the biologically active 26S proteasome for ubiquitin-dependent proteolysis. Both general and dedicated proteasome assembly chaperones regulate the efficiency and outcome of critical steps in proteasome biogenes

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17

Buneeva, O. A., A. T. Kopylov, and A. E. Medvedev. "The key role of the regulatory 19S subunit in changes in the brain proteasome subproteome induced by the neuroprotector isatin." Biomeditsinskaya Khimiya 68, no. 4 (2022): 250–62. http://dx.doi.org/10.18097/pbmc20226804250.

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Isatin (indole-2,3-dione) is an endogenous regulator exhibiting various effects mediated by numerous isatin-binding proteins localized in different compartments of cells of the brain and peripheral tissues. It attenuates manifestations of experimental parkinsonism induced by administration of the MPTP neurotoxin and reduces the movement disorders characteristic of this disease. The molecular mechanisms of the neuroprotective action of isatin include its direct interaction with proteasomes, intracellular supramolecular complexes responsible for the targeted elimination of proteins. Incubation o

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18

Le Tallec, Benoît, Marie-Bénédicte Barrault, Raphaël Guérois, Thibault Carré, and Anne Peyroche. "Hsm3/S5b Participates in the Assembly Pathway of the 19S Regulatory Particle of the Proteasome." Molecular Cell 33, no. 3 (2009): 389–99. http://dx.doi.org/10.1016/j.molcel.2009.01.010.

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19

Winkler, L. L., J. Hwang, and R. F. Kalejta. "Ubiquitin-Independent Proteasomal Degradation of Tumor Suppressors by Human Cytomegalovirus pp71 Requires the 19S Regulatory Particle." Journal of Virology 87, no. 8 (2013): 4665–71. http://dx.doi.org/10.1128/jvi.03301-12.

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20

Steinberger, Shirel, Julia Adler, and Yosef Shaul. "Method of Monitoring 26S Proteasome in Cells Revealed the Crucial Role of PSMA3 C-Terminus in 26S Integrity." Biomolecules 13, no. 6 (2023): 992. http://dx.doi.org/10.3390/biom13060992.

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Proteasomes critically regulate proteostasis via protein degradation. Proteasomes are multi-subunit complexes composed of the 20S proteolytic core particle (20S CP) that, in association with one or two 19S regulatory particles (19S RPs), generates the 26S proteasome, which is the major proteasomal complex in cells. Native gel protocols are used to investigate the 26S/20S ratio. However, a simple method for detecting these proteasome complexes in cells is missing. To this end, using CRISPR technology, we YFP-tagged the endogenous PSMB6 (β1) gene, a 20S CP subunit, and co-tagged endogenous PSMD6

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21

Marquez-Lona, Esther Magdalena, Ana Lilia Torres-Machorro, Frankie R. Gonzales, Lorraine Pillus, and Gentry N. Patrick. "Phosphorylation of the 19S regulatory particle ATPase subunit, Rpt6, modifies susceptibility to proteotoxic stress and protein aggregation." PLOS ONE 12, no. 6 (2017): e0179893. http://dx.doi.org/10.1371/journal.pone.0179893.

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22

Ferdous, Anwarul, Fernando Gonzalez, Liping Sun, Thomas Kodadek, and Stephen Albert Johnston. "The 19S Regulatory Particle of the Proteasome Is Required for Efficient Transcription Elongation by RNA Polymerase II." Molecular Cell 7, no. 5 (2001): 981–91. http://dx.doi.org/10.1016/s1097-2765(01)00250-7.

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23

Truax, Agnieszka Dorota, and Susanna F. Greer. "The role of the 19S ATPase S6a in the transcriptional regulation of major histocompatibility class II (MHC II) genes (35.26)." Journal of Immunology 178, no. 1_Supplement (2007): S6. http://dx.doi.org/10.4049/jimmunol.178.supp.35.26.

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Abstract MHC II molecules are glycoproteins that present intracellular antigens to CD4+ T cells and play an important role in induction and regulation of adaptive immune responses. MHC II molecules are regulated at the level of transcription by a master regulator, the class II transcriptional activator, CIITA, whose association with the MHC promoter is necessary for initiation of transcription. It is well established that one mechanism of regulating transcription is through degradation of factors by the 26S proteasome. The proteasome is composed of a 19S regulatory particle that recognizes ubi

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24

Boehringer, Jonas, Christiane Riedinger, Konstantinos Paraskevopoulos, et al. "Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation." Biochemical Journal 448, no. 1 (2012): 55–65. http://dx.doi.org/10.1042/bj20120542.

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The ubiquitin–proteasome system targets selected proteins for degradation by the 26S proteasome. Rpn12 is an essential component of the 19S regulatory particle and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. In the present paper we report the crystal structure of Rpn12, a proteasomal PCI-domain-containing protein. The structure helps to define a core structural motif for the PCI domain and identifies potential sites through which Rpn12 might form protein–protein interactions. We demonstrate that mutating residues at one of these sites impairs Rpn12 binding to Rpn10 in vi

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25

Kao, Athit, Arlo Randall, Yingying Yang, et al. "Mapping the Structural Topology of the Yeast 19S Proteasomal Regulatory Particle Using Chemical Cross-linking and Probabilistic Modeling." Molecular & Cellular Proteomics 11, no. 12 (2012): 1566–77. http://dx.doi.org/10.1074/mcp.m112.018374.

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Otsubo, Ryota, Hitomi Mimuro, Hiroshi Ashida, Jun Hamazaki, Shigeo Murata, and Chihiro Sasakawa. "Shigellaeffector IpaH4.5 targets 19S regulatory particle subunit RPN13 in the 26S proteasome to dampen cytotoxic T lymphocyte activation." Cellular Microbiology 21, no. 3 (2018): e12974. http://dx.doi.org/10.1111/cmi.12974.

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Bai, Minghui, Xian Zhao, Kazutaka Sahara, et al. "In-depth Analysis of the Lid Subunits Assembly Mechanism in Mammals." Biomolecules 9, no. 6 (2019): 213. http://dx.doi.org/10.3390/biom9060213.

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The 26S proteasome is a key player in the degradation of ubiquitinated proteins, comprising a 20S core particle (CP) and a 19S regulatory particle (RP). The RP is further divided into base and lid subcomplexes, which are assembled independently from each other. We have previously demonstrated the assembly pathway of the CP and the base by observing assembly intermediates resulting from knockdowns of each proteasome subunit and the assembly chaperones. In this study, we examine the assembly pathway of the mammalian lid, which remains to be elucidated. We show that the lid assembly pathway is co

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Divald, Andras, Shaye Kivity, Ping Wang, et al. "Myocardial Ischemic Preconditioning Preserves Postischemic Function of the 26S Proteasome Through Diminished Oxidative Damage to 19S Regulatory Particle Subunits." Circulation Research 106, no. 12 (2010): 1829–38. http://dx.doi.org/10.1161/circresaha.110.219485.

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Matias, Ana C., Paula C. Ramos, and R. Jürgen Dohmen. "Chaperone-assisted assembly of the proteasome core particle." Biochemical Society Transactions 38, no. 1 (2010): 29–33. http://dx.doi.org/10.1042/bst0380029.

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The 26S proteasome is a non-lysosomal protease in the cytosol and nucleus of eukaryotic cells. Its main function is to mediate ubiquitin-dependent proteolysis. The 26S proteasome is a multimeric complex composed by the 20S proteasome CP (core particle) and the 19S RPs (regulatory particles). Although the atomic structure of the 26S proteasome has not yet been determined, high-resolution structures are available for its CP. Studies on the complicated assembly pathway of the proteasome have revealed that it involves an unprecedented number of dedicated chaperones. Assembly of the CP alone involv

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Sun, Shuangwu, Sisi Liu, Zhengmao Zhang, et al. "Phosphatase UBLCP1 controls proteasome assembly." Open Biology 7, no. 5 (2017): 170042. http://dx.doi.org/10.1098/rsob.170042.

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Ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1), an FCP/SCP phosphatase family member, was identified as the first proteasome phosphatase. UBLCP1 binds to proteasome subunit Rpn1 and dephosphorylates the proteasome in vitro . However, it is still unclear which proteasome subunit(s) are the bona fide substrate(s) of UBLCP1 and the precise mechanism for proteasome regulation remains elusive. Here, we show that UBLCP1 selectively binds to the 19S regulatory particle (RP) through its interaction with Rpn1, but not the 20S core particle (CP) or the 26S proteasome holoenzym

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Tonoki, Ayako, Erina Kuranaga, Takeyasu Tomioka, et al. "Genetic Evidence Linking Age-Dependent Attenuation of the 26S Proteasome with the Aging Process." Molecular and Cellular Biology 29, no. 4 (2008): 1095–106. http://dx.doi.org/10.1128/mcb.01227-08.

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ABSTRACT The intracellular accumulation of unfolded or misfolded proteins is believed to contribute to aging and age-related neurodegenerative diseases. However, the links between age-dependent proteotoxicity and cellular protein degradation systems remain poorly understood. Here, we show that 26S proteasome activity and abundance attenuate with age, which is associated with the impaired assembly of the 26S proteasome with the 19S regulatory particle (RP) and the 20S proteasome. In a genetic gain-of-function screen, we characterized Rpn11, which encodes a subunit of the 19S RP, as a suppressor

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Takahashi, M., H. Iwasaki, H. Inoue, and K. Takahashi. "Reverse Genetic Analysis of the Caenorhabditis elegans 26S Proteasome Subunits by RNA Interference." Biological Chemistry 383, no. 7-8 (2002): 1263–66. http://dx.doi.org/10.1515/bc.2002.140.

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Abstract Reverse genetic analysis was performed on the Caenorhabditis elegans 26S proteasome subunit genes by doublestranded RNAmediated interference (RNAi). Embryonic and postembryonic lethality was caused by interference of all of the eight tested 20S core subunits and all of the 19S regulatory particle subunits except for CeRpn9, CeRpn10, and Ce Rpn12, where RNAi caused no abnormality. However, synthetic suppression of CeRpn10 and CeRpn12 was lethal, whereas neither the combination of Ce Rpn9 with CeRpn10 nor with CeRpn12 resulted in abnormalities in RNAi. These results indicate that the 26

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Yue, Xin, Yinglin Zuo, Hongpeng Ke, et al. "Identification of 4-arylidene curcumin analogues as novel proteasome inhibitors for potential anticancer agents targeting 19S regulatory particle associated deubiquitinase." Biochemical Pharmacology 137 (August 2017): 29–50. http://dx.doi.org/10.1016/j.bcp.2017.04.032.

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Liu, Xiaoyan, Weidi Xiao, Yanan Zhang, et al. "Reversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function." Proceedings of the National Academy of Sciences 117, no. 1 (2019): 328–36. http://dx.doi.org/10.1073/pnas.1912531117.

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The fundamental importance of the 26S proteasome in health and disease suggests that its function must be finely controlled, and yet our knowledge about proteasome regulation remains limited. Posttranslational modifications, especially phosphorylation, of proteasome subunits have been shown to impact proteasome function through different mechanisms, although the vast majority of proteasome phosphorylation events have not been studied. Here, we have characterized 1 of the most frequently detected proteasome phosphosites, namely Ser361 of Rpn1, a base subunit of the 19S regulatory particle. Usin

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Bustamante, Hianara A., Karina Cereceda, Alexis E. González, et al. "The Proteasomal Deubiquitinating Enzyme PSMD14 Regulates Macroautophagy by Controlling Golgi-to-ER Retrograde Transport." Cells 9, no. 3 (2020): 777. http://dx.doi.org/10.3390/cells9030777.

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Ubiquitination regulates several biological processes, however the role of specific members of the ubiquitinome on intracellular membrane trafficking is not yet fully understood. Here, we search for ubiquitin-related genes implicated in protein membrane trafficking performing a High-Content siRNA Screening including 1187 genes of the human “ubiquitinome” using amyloid precursor protein (APP) as a reporter. We identified the deubiquitinating enzyme PSMD14, a subunit of the 19S regulatory particle of the proteasome, specific for K63-Ub chains in cells, as a novel regulator of Golgi-to-endoplasmi

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Lim, Hyun-Suk, Di Cai, Chase T. Archer, and Thomas Kodadek. "Periodate-Triggered Cross-Linking Reveals Sug2/Rpt4 as the Molecular Target of a Peptoid Inhibitor of the 19S Proteasome Regulatory Particle." Journal of the American Chemical Society 129, no. 43 (2007): 12936–37. http://dx.doi.org/10.1021/ja075469+.

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Shibahara, Tadashi, Hiroshi Kawasaki, and Hisashi Hirano. "Mass spectrometric analysis of expression of ATPase subunits encoded by duplicated genes in the 19S regulatory particle of rice 26S proteasome." Archives of Biochemistry and Biophysics 421, no. 1 (2004): 34–41. http://dx.doi.org/10.1016/j.abb.2003.10.013.

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Gu, Yanyan, Benjamin G. Barwick, Mala Shanmugam та ін. "The Role of Proteasome Activator PA28α in Multiple Myeloma". Blood 134, Supplement_1 (2019): 5499. http://dx.doi.org/10.1182/blood-2019-128216.

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Multiple myeloma (MM) is a commonly occurring hematologic malignancy in the United States with poor prognosis. Among all treatments, proteasome inhibitor (PI) based regimens have been a major breakthrough for patients' outcomes. Available PIs all target 20S proteasome core complex, and the duration of response is limited by toxicity and resistance development. Until now, the underlying mechanism of drug resistance remains unclear. The proteasome is the major proteolytic machinery in protein homeostasis which is pivotal for myeloma cell survival. A functional proteasome consists of 20S proteaso

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Diao, Wentao, Xue Yang, and Hao Zhou. "Purification, crystallization and preliminary X-ray data collection of the N-terminal domain of the 26S proteasome regulatory subunit p27 and its complex with the ATPase domain of Rpt5 fromMus musculus." Acta Crystallographica Section F Structural Biology Communications 70, no. 5 (2014): 611–15. http://dx.doi.org/10.1107/s2053230x14006815.

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The protein 26S proteasome regulatory subunit p27 is one of the four chaperones that help in the assembly of the 19S regulatory particle (RP) of the 26S proteasome. In the present work, the N-terminus of p27 (residues 1–128) fromMus musculuswas cloned, expressed, purified and crystallized alone and in complex with the C-terminal ATPase domain of Rpt5 (residues 173–442). The crystals of p27(1–128)diffracted to 1.7 Å resolution and belonged to space groupP212121, with unit-cell parametersa= 26.79,b= 30.39,c= 145.06 Å. Resolution-dependent Matthews coefficient probability analysis suggested the p

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Song, Yan, Arghya Ray, Deepika Sharma DAS, Dharminder Chauhan, and Kenneth C. Anderson. "Targeting 19S-Proteasome Deubiquitinase Rpn11/POH1/PSMD14 in Multiple Myeloma." Blood 126, no. 23 (2015): 1811. http://dx.doi.org/10.1182/blood.v126.23.1811.1811.

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Abstract Introduction Deregulation of the ubiquitin-proteasome system (UPS) is linked to pathogenesis of various human diseases, including cancer. Targeting the proteasome is an effective therapy in multiple myeloma (MM) patients. Recent research efforts led to the discovery of newer agents that target enzymes modulating protein ubiquitin-conjugation/deconjugation rather than the proteasome itself, with the goal of generating more specific and less toxic antitumor therapies. Ubiquitylation is a dynamic reversible process coordinated by many enzymes: ubiquitin ligases attach ubiquitin to protei

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Kuo, Chueh-Ling, and Alfred Lewis Goldberg. "Ubiquitinated proteins promote the association of proteasomes with the deubiquitinating enzyme Usp14 and the ubiquitin ligase Ube3c." Proceedings of the National Academy of Sciences 114, no. 17 (2017): E3404—E3413. http://dx.doi.org/10.1073/pnas.1701734114.

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In mammalian cells, the 26S proteasomes vary in composition. In addition to the standard 28 subunits in the 20S core particle and 19 subunits in each 19S regulatory particle, a small fraction (about 10–20% in our preparations) also contains the deubiquitinating enzyme Usp14/Ubp6, which regulates proteasome activity, and the ubiquitin ligase, Ube3c/Hul5, which enhances proteasomal processivity. When degradation of ubiquitinated proteins in cells was inhibited, levels of Usp14 and Ube3c on proteasomes increased within minutes. Conversely, when protein ubiquitination was prevented, or when purifi

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Xia, Xue, Chun-Meng Tang, Gu-Zi Chen, and Jia-Jia Han. "Proteasome Dysfunction Leads to Suppression of the Hypoxic Response Pathway in Arabidopsis." International Journal of Molecular Sciences 23, no. 24 (2022): 16148. http://dx.doi.org/10.3390/ijms232416148.

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Proteasome is a large proteolytic complex that consists of a 20S core particle (20SP) and 19S regulatory particle (19SP) in eukaryotes. The proteasome degrades most cellular proteins, thereby controlling many key processes, including gene expression and protein quality control. Proteasome dysfunction in plants leads to abnormal development and reduced adaptability to environmental stresses. Previous studies have shown that proteasome dysfunction upregulates the gene expression of proteasome subunits, which is known as the proteasome bounce-back response. However, the proteasome bounce-back res

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Sahu, Indrajit, and Michael H. Glickman. "Proteasome in action: substrate degradation by the 26S proteasome." Biochemical Society Transactions 49, no. 2 (2021): 629–44. http://dx.doi.org/10.1042/bst20200382.

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Ubiquitination is the major criteria for the recognition of a substrate-protein by the 26S proteasome. Additionally, a disordered segment on the substrate — either intrinsic or induced — is critical for proteasome engagement. The proteasome is geared to interact with both of these substrate features and prepare it for degradation. To facilitate substrate accessibility, resting proteasomes are characterised by a peripheral distribution of ubiquitin receptors on the 19S regulatory particle (RP) and a wide-open lateral surface on the ATPase ring. In this substrate accepting state, the internal ch

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Muller, D. "A molecular link A molecular link between Hairless and Pros26.4, a member of the AAA-ATPase subunits of the proteasome 19S regulatory particle in Drosophila." Journal of Cell Science 119, no. 2 (2006): 250–58. http://dx.doi.org/10.1242/jcs.02743.

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Fang, Teng, Yan Song, Ting Du, et al. "26S Proteasome Non-Atpase Subunit 3 (PSMD3/Rpn3) Is a Potential Therapeutic Target in Multiple Myeloma." Blood 144, Supplement 1 (2024): 1905. https://doi.org/10.1182/blood-2024-206000.

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Background and Rationale: Multiple myeloma (MM) is a cancer of the plasma cells characterized by excessive production of immunoglobulins and dependence on the protein degradation system, which makes proteasome inhibitors (PIs) an important treatment for MM patients. However, PI resistance remains an unsolved problem in MM. PIs directly target the 20S core particle (CP) of the proteasome, which is responsible for proteolysis. The 19S regulatory particle (RP) is another component of the 26S proteasome that identifies ubiquitinated proteins and directs them to the 20S CP for degradation. We hypot

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Cekała, Katarzyna, Karolina Trepczyk, Julia Witkowska, Elżbieta Jankowska, and Ewa Wieczerzak. "Rpt5-Derived Analogs Stimulate Human Proteasome Activity in Cells and Degrade Proteins Forming Toxic Aggregates in Age-Related Diseases." International Journal of Molecular Sciences 25, no. 9 (2024): 4663. http://dx.doi.org/10.3390/ijms25094663.

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Aging and age-related diseases are associated with a decline in the capacity of protein turnover. Intrinsically disordered proteins, as well as proteins misfolded and oxidatively damaged, prone to aggregation, are preferentially digested by the ubiquitin-independent proteasome system (UIPS), a major component of which is the 20S proteasome. Therefore, boosting 20S activity constitutes a promising strategy to counteract a decrease in total proteasome activity during aging. One way to enhance the proteolytic removal of unwanted proteins appears to be the use of peptide-based activators of the 20

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McDonald, Heather B., Astrid Hoes Helfant, Erin M. Mahony, Shaun K. Khosla, and Loretta Goetsch. "Mutational Analysis Reveals a Role for the C Terminus of the Proteasome Subunit Rpt4p in Spindle Pole Body Duplication inSaccharomyces cerevisiae." Genetics 162, no. 2 (2002): 705–20. http://dx.doi.org/10.1093/genetics/162.2.705.

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AbstractThe ubiquitin/proteasome pathway plays a key role in regulating cell cycle progression. Previously, we reported that a conditional mutation in the Saccharomyces cerevisiae gene RPT4/PCS1, which encodes one of six ATPases in the proteasome 19S cap complex/regulatory particle (RP), causes failure of spindle pole body (SPB) duplication. To improve our understanding of Rpt4p, we created 58 new mutations, 53 of which convert clustered, charged residues to alanine. Virtually all mutations that affect the N-terminal region, which contains a putative nuclear localization signal and coiled-coil

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Li, Shuyu, Robert A. Spooner, Stuart C. H. Allen, et al. "Folding-competent and Folding-defective Forms of Ricin A Chain Have Different Fates after Retrotranslocation from the Endoplasmic Reticulum." Molecular Biology of the Cell 21, no. 15 (2010): 2543–54. http://dx.doi.org/10.1091/mbc.e09-08-0743.

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We report that a toxic polypeptide retaining the potential to refold upon dislocation from the endoplasmic reticulum (ER) to the cytosol (ricin A chain; RTA) and a misfolded version that cannot (termed RTAΔ), follow ER-associated degradation (ERAD) pathways in Saccharomyces cerevisiae that substantially diverge in the cytosol. Both polypeptides are dislocated in a step mediated by the transmembrane Hrd1p ubiquitin ligase complex and subsequently degraded. Canonical polyubiquitylation is not a prerequisite for this interaction because a catalytically inactive Hrd1p E3 ubiquitin ligase retains t

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McPherson, Ann, and Tania Watts. "The role of TRAF1 in stabilizing TRAF2 from proteasome mediated degradation downstream of 4-1BB signaling (138.1)." Journal of Immunology 184, no. 1_Supplement (2010): 138.1. http://dx.doi.org/10.4049/jimmunol.184.supp.138.1.

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Abstract TNF receptor family members play important roles in the innate and adaptive immune response, inducing signals for cell survival or apoptosis. This signaling in most cases relies on TNF receptor associated factors (TRAFs) to relay the signal from the TNFR family member to activation of NF-κB or MAPK pathways. Results from our lab have shown that TRAF1 is critical in the downregulation of the proapoptotic molecule Bim and the survival of activated and memory CD8 T cells, acting downstream of the prosurvival TNF receptor family member 4-1BB. We show here that in the absence of TRAF1, sig

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Lokireddy, Sudarsanareddy, Nikolay Vadimovich Kukushkin, and Alfred Lewis Goldberg. "cAMP-induced phosphorylation of 26S proteasomes on Rpn6/PSMD11 enhances their activity and the degradation of misfolded proteins." Proceedings of the National Academy of Sciences 112, no. 52 (2015): E7176—E7185. http://dx.doi.org/10.1073/pnas.1522332112.

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Although rates of protein degradation by the ubiquitin-proteasome pathway (UPS) are determined by their rates of ubiquitination, we show here that the proteasome’s capacity to degrade ubiquitinated proteins is also tightly regulated. We studied the effects of cAMP-dependent protein kinase (PKA) on proteolysis by the UPS in several mammalian cell lines. Various agents that raise intracellular cAMP and activate PKA (activators of adenylate cyclase or inhibitors of phosphodiesterase 4) promoted degradation of short-lived (but not long-lived) cell proteins generally, model UPS substrates having di

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