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26S proteasome

Jianhua Huang, Chipan Zhu, Xin Li
In mammals, tumor necrosis factor receptor associated factors (TRAFs) are signaling adaptors that regulate diverse physiological processes, including immunity and stress responses. In Arabidopsis, MUSE13 and MUSE14 are redundant TRAF proteins serving as adaptors in the SCFCRP 1 complex to facilitate the turnover of nucleotide-binding domain and leucine-rich repeats (NLR) immune receptors. Degradation of MUSE13 is inhibited by proteasome inhibitor, suggesting that the MUSE13 stability is controlled by the 26S proteasome...
May 16, 2018: Plant Journal: for Cell and Molecular Biology
Mariah L Farrell, Michaela R Reagan
It is becoming clear that myeloma cell-induced disruption of the highly organized bone marrow components (both cellular and extracellular) results in destruction of the marrow and support for multiple myeloma (MM) cell proliferation, survival, migration, and drug resistance. Since the first phase I clinical trial on bortezomib was published 15 years ago, proteasome inhibitors (PIs) have become increasingly common for treatment of MM and are currently an essential part of any anti-myeloma combination therapy...
2018: Frontiers in Endocrinology
Jung Hoon Lee, Seoyoung Park, Yejin Yun, Won Hoon Choi, Min-Ji Kang, Min Jae Lee
BACKGROUND/AIMS: The 26S proteasome is the key proteolytic complex for recognition and degradation of polyubiquitinated target substrates in eukaryotes. Among numerous proteasome-associated proteins, a deubiquitinating enzyme (DUB) USP14 has been identified as an endogenous inhibitor of the proteasome. Here, we explored the complex regulatory functions of USP14 that involve ubiquitin (Ub) homeostasis and substrate degradation in flies and mammals. METHODS: USP14-null primary and immortalized mouse embryonic fibroblasts (MEFs) and USP14 knocked-down Drosophila were analyzed in this study...
May 9, 2018: Cellular Physiology and Biochemistry
Ingrid Gerke, Franz-Josef Kaup, Stephan Neumann
Studies in humans have shown that the ubiquitin-proteasome pathway and the insulin-like growth factor axis are involved in carcinogenesis, thus, components of these systems might be useful as prognostic markers and constitute potential therapeutic targets. In veterinary medicine, only a few studies exist on this topic. Here, serum concentrations of 26S proteasome (26SP) and insulin-like growth factor-1 (IGF-1) were measured by canine enzyme-linked immunosorbent assay (ELISA) in 43 dogs suffering from malignant tumors and 21 clinically normal dogs (control group)...
April 2018: Canadian Journal of Veterinary Research, Revue Canadienne de Recherche Vétérinaire
Tae Ho Kim, Jun-Yong Choi, Kyun Ha Kim, Min Jung Kwun, Chang-Woo Han, Ran Won, Jung Ju Lee, Jong-In Kim, Myungsoo Joo
Hominis placenta (HP), a dried human placenta, has been known to target liver, lung, or kidney meridians, improving the functions associated with these meridians in traditional Chinese or Asian medicine (TCM). Since recent studies implicate an HP extract in suppressing inflammation, we investigated whether an aqueous HP extract can ameliorate inflammation that occurred in the lungs. When administered with a single intratracheal lipopolysaccharide (LPS), C57BL/6 mice developed an acute neutrophilic lung inflammation along with an increased expression of pro-inflammatory cytokine genes...
May 13, 2018: American Journal of Chinese Medicine
Ingrid Gerke, Franz-Josef Kaup, Stephan Neumann
In patients suffering from chronic diseases, the objective assessment of metabolic states could be of interest for disease prognosis and therapeutic options. Therefore, the aim of this study was to assess insulin-like growth factor-1 (IGF-1) and 26S proteasome (26SP) in healthy dogs and dogs suffering from chronic diseases depending on their body condition score (BCS) and to examine their potential for objective assessment of anabolic and catabolic states. Serum concentrations of IGF-1, an anabolic hormone, and 26SP, a multiprotein complex which is part of the ubiquitin-proteasome pathway, by which the majority of endogenous proteins including the muscle proteins are degraded, were measured in 21 healthy dogs and 20 dogs with chronic diseases by canine ELISA...
April 26, 2018: Research in Veterinary Science
Yun Yun Zhou, Rachel Ka Man Chun, Jian Chao Wang, Bing Zuo, King Kit Li, Thomas Chuen Lam, Quan Liu, Chi-Ho To
Myopia development has been extensively studied from different perspectives. Myopia recovery is also considered important for understanding the development of myopia. However, despite several previous studies, retinal proteomics during recovery from myopia is still relatively unknown. Therefore, the aim of the present study was to investigate the changes in protein profiles of chicken retinas during early recovery from lens‑induced myopia to evaluate the signals involved in the adjustment of this refractive disorder...
May 3, 2018: Molecular Medicine Reports
Geeta Rao, Hailey Houson, Gregory Nkepang, Hooman Yari, Chengwen Teng, Vibhudutta Awasthi
BACKGROUND: Multi-organ failure in hemorrhagic shock is triggered by gut barrier dysfunction and consequent systemic infiltration of proinflammatory factors. Our previous study has shown that diphenyldihaloketone drugs CLEFMA and EF24 restore gut barrier dysfunction and reduce systemic inflammatory response in hemorrhagic shock. AIMS: We investigated the effect of hemorrhagic shock on proteasome activity of intestinal epithelium and how CLEFMA and EF24 treatments modulate proteasome function in hemorrhagic shock...
May 10, 2018: American Journal of Physiology. Gastrointestinal and Liver Physiology
Tian-Xia Jiang, Mei Zhao, Xiao-Bo Qiu
Proteasomes are responsible for the turnover of most cellular proteins, and thus are critical to almost all cellular activities. A substrate entering the proteasome must first bind to a substrate receptor. Substrate receptors can be classified as ubiquitin receptors and non-ubiquitin receptors. The intrinsic ubiquitin receptors, including proteasome regulatory particle base subunits 1, 10 and 13 (Rpn1, Rpn10, and Rpn13), determine the capability of the proteasome to recognize a ubiquitin chain, and thus provide selectivity for the 26S proteasome...
May 6, 2018: Biological Reviews of the Cambridge Philosophical Society
O A Buneeva, A E Medvedev
Proteasomes are large supramolecular protein complexes present in all prokaryotic and eukaryotic cells, where they perform targeted degradation of intracellular proteins. Until recently, it was generally accepted that prior proteolytic degradation in proteasomes the proteins had to be targeted by ubiquitination: the ATP-dependent addition of (typically four sequential) residues of the low-molecular ubiquitin protein, involving the ubiquitin-activating enzyme, ubiquitin-conjugating enzyme and ubiquitin ligase...
March 2018: Biomedit︠s︡inskai︠a︡ Khimii︠a︡
Avi Levin, Adi Minis, Gadi Lalazar, Jose Rodriguez, Hermann Steller
Protein degradation by the ubiquitin-proteasome system (UPS) is central to protein homeostasis and cell survival. The active 26S proteasome is a large protease complex consisting of a catalytic 20S subunit and 19S regulatory particles. Cancer cells are exposed to considerable protein overload due to high metabolic rates, reprogrammed energy metabolism and aneuploidy. Here we report a mechanism that facilitates the assembly of active 26S proteasomes in malignant cells. Upon tumorigenic transformation of the gut epithelium, 26S proteasome assembly was significantly enhanced, but levels of individual subunits were not changed...
May 1, 2018: Cancer Research
Silvia Grottelli, Egidia Costanzi, Matthew J Peirce, Alba Minelli, Barbara Cellini, Ilaria Bellezza
Protein function is dependent on assumption of the correct three-dimensional structure, achieved through the folding process. As a central element in ensuring cellular homeostasis, proteostasis i.e. the control of correct protein folding, trafficking and degradation, is a highly regulated process ensured by three integrated molecular pathways: i) the unfolded protein response (UPR) which is activated by the engulfment of misfolded proteins and results in protein re-folding through the expression of chaperones; ii) the ubiquitin-proteasome system (UPS) which 'flags' misfolded proteins with ubiquitin, directing them to the 26S proteasome for proteolytic degradation; iii) autophagy that, through lysosomes, removes misfolded or aggregated proteins...
April 30, 2018: Current Protein & Peptide Science
Shalon E Babbitt, Alexi Kiss, Andrew E Deffenbaugh, Yie-Hwa Chang, Eric Bailly, Hediye Erdjument-Bromage, Paul Tempst, Tione Buranda, Larry A Sklar, Jennifer Baumler, Edward Gogol, Dorota Skowyra
No abstract text is available yet for this article.
April 19, 2018: Cell
Lele Wang, Linlin Zhao, Guo Wei, Dieter Saur, Barbara Seidler, Junyan Wang, Chuanxin Wang, Tonggang Qi
Pancreatic ductal adenocarcinoma (PDAC) remains one of the most devastating disease with the 5-year survival rate less than 6%. In this study, we investigated if inhibiting protein synthesis directly with homoharringtonine (HHT) could induce acute apoptosis in pancreatic cancer cells through quick depletion of multiple short-lived critical members of the central proteome, example, PSMD11(26S proteasome non-ATPase regulatory subunit 11). It was shown that although HHT could inhibit proliferation and growth of MiaPaCa-2 and PANC-1 cells in a time- and dose-dependent manner, only part of pancreatic cancer cells could be induced to die through acute apoptosis...
April 17, 2018: Journal of Cellular Biochemistry
Joo Yong Kim, Bong Soo Park, Sang Woo Park, Han Yong Lee, Jong Tae Song, Hak Soo Seo
Nitrate reductases (NRs) catalyze the first step in the reduction of nitrate to ammonium. NR activity is regulated by sumoylation through the E3 ligase activity of AtSIZ1. However, it is not clear how NRs interact with AtSIZ1 in the cell, or how nitrogen sources affect NR levels and their cellular localization. Here, we show that the subcellular localization of NRs is modulated by the E3 SUMO (Small ubiquitin-related modifier) ligase AtSIZ1 and that NR protein levels are regulated by nitrogen sources. Transient expression analysis of GFP fusion proteins in onion epidermal cells showed that the NRs NIA1 and NIA2 localize to the cytoplasmic membrane, and that AtSIZ1 localizes to the nucleoplasm, including nuclear bodies, when expressed separately, whereas NRs and AtSIZ1 localize to the nucleus when co-expressed...
April 15, 2018: International Journal of Molecular Sciences
Ji Jiang, Lok Ming Tam, Pengcheng Wang, Yinsheng Wang
Activation of the nuclear factor erythroid 2-related factor 2 (Nrf2) antioxidant response signaling pathway is a major mechanism for the cellular defense against oxidative stress. Arsenite, a widespread contaminant in drinking water, is known to induce oxidative stress and activate Nrf2-dependent signaling pathway through stabilization of Nrf2 protein by inhibiting its ubiquitination via the Cul3-Rbx1-Keap1 (cullin 3, RING-box 1, and Kelch-like ECH-associated protein 1) E3 ubiquitin ligase and its degradation by the 26S proteasome, though the underlying mechanism remains elusive...
April 16, 2018: Chemical Research in Toxicology
Jared A M Bard, Ellen A Goodall, Eric R Greene, Erik Jonsson, Ken C Dong, Andreas Martin
As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The proteasome's cellular functions range from general protein homeostasis and stress response to the control of vital processes such as cell division and signal transduction. To reliably process all the proteins presented to it in the complex cellular environment, the proteasome must combine high promiscuity with exceptional substrate selectivity...
April 13, 2018: Annual Review of Biochemistry
Richard Scott Marshall, Richard David Vierstra
26S proteasome abundance is tightly regulated at multiple levels, including the elimination of excess or inactive particles by autophagy. In yeast, this proteaphagy occurs upon nitrogen starvation but not carbon starvation, which instead stimulates the rapid sequestration of proteasomes into cytoplasmic puncta termed proteasome storage granules (PSGs). Here, we show that PSGs help protect proteasomes from autophagic degradation. Both the core protease and regulatory particle sub-complexes are sequestered separately into PSGs via pathways dependent on the accessory proteins Blm10 and Spg5, respectively...
April 6, 2018: ELife
Zhenchuan Chen, Wei Zhang, Zhimin Yun, Xue Zhang, Feng Gong, Yunfang Wang, Shouping Ji, Ling Leng
In response to DNA damage, proliferating cell nuclear antigen (PCNA) has an important role as a positive regulator and as a scaffold protein associated with DNA damage bypass and repair pathways by serving as a platform for the recruitment of associated components. As demonstrated in the present study, the ubiquitin‑like modifier human leukocyte antigen F locus adjacent transcript 10 (FAT10), which binds to PCNA but has not previously been demonstrated to be associated with the DNA damage response (DDR), is induced by ultraviolet/ionizing radiation and VP‑16 treatment in HeLa cells...
April 5, 2018: Molecular Medicine Reports
Shaughna Langerak, Myung-Jun Kim, Hannah Lamberg, Michael Godinez, Mackenzie Main, Lindsey Winslow, Michael B O'Connor, Changqi C Zhu
The Drosophila Activin signaling pathway employs at least three separate ligands, Activin-β (Actβ), Dawdle (Daw), and Myoglianin (Myo), to regulate several general aspects of fruit fly larval development including cell proliferation, neuronal remodeling, and metabolism. Here we provide experimental evidence indicating that both Daw and Myo are anti-ageing factors in adult fruit flies. Knockdown of Myo or Daw in adult fruit flies reduced mean lifespan, while overexpression of either ligand in adult muscle tissues but not in adipose tissues enhanced mean lifespan...
April 3, 2018: Biology Open
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