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26S proteasome

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https://www.readbyqxmd.com/read/27898393/a-noncanonical-auxin-sensing-mechanism-is-required-for-organ-morphogenesis-in-arabidopsis
#1
Sara Simonini, Joyita Deb, Laila Moubayidin, Pauline Stephenson, Manoj Valluru, Alejandra Freire-Rios, Karim Sorefan, Dolf Weijers, Jiří Friml, Lars Østergaard
Tissue patterning in multicellular organisms is the output of precise spatio-temporal regulation of gene expression coupled with changes in hormone dynamics. In plants, the hormone auxin regulates growth and development at every stage of a plant's life cycle. Auxin signaling occurs through binding of the auxin molecule to a TIR1/AFB F-box ubiquitin ligase, allowing interaction with Aux/IAA transcriptional repressor proteins. These are subsequently ubiquitinated and degraded via the 26S proteasome, leading to derepression of auxin response factors (ARFs)...
October 15, 2016: Genes & Development
https://www.readbyqxmd.com/read/27888613/psmc2-is-up-regulated-in-osteosarcoma-and-regulates-osteosarcoma-cell-proliferation-apoptosis-and-migration
#2
Mingzhi Song, Yong Wang, Zhen Zhang, Shouyu Wang
Proteasome 26S subunit ATPase 2 (PSMC2) is a recently identified gene potentially associated with certain human carcinogenesis. However, the expressional correlation and functional importance of PSMC2 in osteosarcoma is still unclear. Current study was focused on elucidating the significance of PSMC2 on malignant behaviors in osteosarcoma including proliferation, apoptosis, colony formation, migration as well as invasion. The high protein levels of PSMC2 in osteosarcoma samples were identified by tissue microarrays analysis...
November 23, 2016: Oncotarget
https://www.readbyqxmd.com/read/27881664/lipid-disequilibrium-disrupts-er-proteostasis-by-impairing-erad-substrate-glycan-trimming-and-dislocation
#3
Milton To, Clark W H Peterson, Melissa A Roberts, Jessica L Counihan, Tiffany T Wu, Mercedes S Forster, Daniel K Nomura, James A Olzmann
The endoplasmic reticulum (ER) mediates the folding, maturation, and deployment of the secretory proteome. Proteins that fail to achieve their native conformation are retained in the ER and targeted for clearance by ER-associated degradation (ERAD), a sophisticated process that mediates the ubiquitin-dependent delivery of substrates to the 26S proteasome for proteolysis. Recent findings indicate that inhibition of long-chain acyl-CoA synthetases with triacsin C, a fatty acid analog, impairs lipid droplet (LD) biogenesis and ERAD, suggesting a role for LDs in ERAD...
November 23, 2016: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/27875560/denervation-induced-activation-of-the-standard-proteasome-and-immunoproteasome
#4
Haiming M Liu, Deborah A Ferrington, Cory W Baumann, LaDora V Thompson
The standard 26S proteasome is responsible for the majority of myofibrillar protein degradation leading to muscle atrophy. The immunoproteasome is an inducible form of the proteasome. While its function has been linked to conditions of atrophy, its contribution to muscle proteolysis remains unclear. Therefore, the purpose of this study was to determine if the immunoproteasome plays a role in skeletal muscle atrophy induced by denervation. Adult male C57BL/6 wild type (WT) and immunoproteasome knockout lmp7-/-/mecl-1-/- (L7M1) mice underwent tibial nerve transection on the left hindlimb for either 7 or 14 days, while control mice did not undergo surgery...
2016: PloS One
https://www.readbyqxmd.com/read/27872216/the-effect-of-temperature-adaptation-on-the-ubiquitin-proteasome-pathway-in-notothenioid-fishes
#5
Anne E Todgham, Timothy A Crombie, Gretchen E Hofmann
There is an accumulating body of evidence suggesting that the sub-zero Antarctic marine environment places physiological constraints on protein homeostasis. Levels of ubiquitin (Ub)-conjugated proteins, 20S proteasome activity and mRNA expression of many proteins involved in both the ubiquitin (Ub) tagging of damaged proteins as well as the different complexes of the 26S proteasome were measured to examine whether there is thermal compensation of the Ub-proteasome pathway in Antarctic fishes to better understand the efficiency of the protein degradation machinery in polar species...
November 21, 2016: Journal of Experimental Biology
https://www.readbyqxmd.com/read/27869775/plant-virus-infection-and-the-ubiquitin-proteasome-machinery-arms-race-along-the-endoplasmic-reticulum
#6
REVIEW
Jeanmarie Verchot
The endoplasmic reticulum (ER) is central to plant virus replication, translation, maturation, and egress. Ubiquitin modification of ER associated cellular and viral proteins, alongside the actions of the 26S proteasome, are vital for the regulation of infection. Viruses can arrogate ER associated ubiquitination as well as cytosolic ubiquitin ligases with the purpose of directing the ubiquitin proteasome system (UPS) to new targets. Such targets include necessary modification of viral proteins which may stabilize certain complexes, or modification of Argonaute to suppress gene silencing...
November 19, 2016: Viruses
https://www.readbyqxmd.com/read/27856401/escrt-i-component-vps23a-affects-aba-signaling-by-recognizing-aba-receptors-for-endosomal-degradation
#7
Feifei Yu, Lijuan Lou, Miaomiao Tian, Qingliang Li, Yanglin Ding, Xiaoqiang Cao, Yaorong Wu, Borja Belda-Palazon, Pedro L Rodriguez, Shuhua Yang, Qi Xie
The recent discovery of PYR/PYL/RCAR-type ABA receptors has been one of most significant advances in plant science. In mammals, endosome sorting acts as an important pathway to down-regulate different types of receptors, but this kind of regulation of hormone signaling is poorly understood in plants. Here, we report that an ubiquitin E2-like protein, VPS23A, also a key component of ESCRT-I, negatively regulates ABA signaling. VPS23A has epistatic relation with PYR/PYL/RCAR type ABA receptors and deletion of VPS23A enhances the activity of key kinase OST1 in ABA signaling pathway under ABA treatment...
November 14, 2016: Molecular Plant
https://www.readbyqxmd.com/read/27852068/fibroblast-growth-factor-signalling-induces-loss-of-progesterone-receptor-in-breast-cancer-cells
#8
Dominika Piasecka, Kamila Kitowska, Dominika Czaplinska, Kamil Mieczkowski, Magdalena Mieszkowska, Lukasz Turczyk, Andrzej C Skladanowski, Anna J Zaczek, Wojciech Biernat, Radzislaw Kordek, Hanna M Romanska, Rafal Sadej
We have recently demonstrated that, fibroblast growth factor 2 (FGFR2), signalling via ribosomal S6 kinase 2 (RSK2), promotes progression of breast cancer (BCa). Loss of progesterone receptor (PR), whose activity in BCa cells can be stimulated by growth factor receptors (GFRs), is associated with poor patient outcome. Here we showed that FGF7/FGFR2 triggered phosphorylation of PR at Ser294, PR ubiquitination and subsequent receptor`s degradation via the 26S proteasome pathway in BCa cells. We further demonstrated that RSK2 mediated FGF7/FGFR2-induced PR downregulation...
November 12, 2016: Oncotarget
https://www.readbyqxmd.com/read/27800122/subnormothermic-perfusion-in-the-isolated-rat-liver-preserves-the-antioxidant-glutathione-and-enhances-the-function-of-the-ubiquitin-proteasome-system
#9
Teresa Carbonell, Norma Alva, Sergio Sanchez-Nuño, Shannamar Dewey, Aldrin V Gomes
The reduction of oxidative stress is suggested to be one of the main mechanisms to explain the benefits of subnormothermic perfusion against ischemic liver damage. In this study we investigated the early cellular mechanisms induced in isolated rat livers after 15 min perfusion at temperatures ranging from normothermia (37°C) to subnormothermia (26°C and 22°C). Subnormothermic perfusion was found to maintain hepatic viability. Perfusion at 22°C raised reduced glutathione levels and the activity of glutathione reductase; however, lipid and protein oxidation still occurred as determined by malondialdehyde, 4-hydroxynonenal-protein adducts, and advanced oxidation protein products...
2016: Oxidative Medicine and Cellular Longevity
https://www.readbyqxmd.com/read/27791183/p62-and-ubiquitin-dependent-stress-induced-autophagy-of-the-mammalian-26s-proteasome
#10
Victoria Cohen-Kaplan, Ido Livneh, Noa Avni, Bertrand Fabre, Tamar Ziv, Yong Tae Kwon, Aaron Ciechanover
The ubiquitin-proteasome system and autophagy are the two main proteolytic systems involved in, among other functions, the maintenance of cell integrity by eliminating misfolded and damaged proteins and organelles. Both systems remove their targets after their conjugation with ubiquitin. An interesting, yet incompletely understood problem relates to the fate of the components of the two systems. Here we provide evidence that amino acid starvation enhances polyubiquitination on specific sites of the proteasome, a modification essential for its targeting to the autophagic machinery...
October 17, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/27791164/structural-basis-for-dynamic-regulation-of-the-human-26s-proteasome
#11
Shuobing Chen, Jiayi Wu, Ying Lu, Yong-Bei Ma, Byung-Hoon Lee, Zhou Yu, Qi Ouyang, Daniel J Finley, Marc W Kirschner, Youdong Mao
The proteasome is the major engine of protein degradation in all eukaryotic cells. At the heart of this machine is a heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitylated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. Using cryoelectron microscopy, we determined a near-atomic-resolution structure of the 2.5-MDa human proteasome in its ground state, as well as subnanometer-resolution structures of the holoenzyme in three alternative conformational states...
October 21, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/27787902/ubc18-mediates-erf1-degradation-under-light-dark-cycles
#12
Mei-Chun Cheng, Wen-Chieh Kuo, Yi-Ming Wang, Hsing-Yu Chen, Tsan-Piao Lin
Ethylene Response Factor 1 (ERF1) plays a crucial role in biotic and abiotic stress responses. Previous studies have shown that ERF1 regulates stress-responsive gene expression by binding to different cis-acting elements in response to various stress signals. ERF1 was also reported to be unstable in the dark, and it regulates hypocotyl elongation. Here, we elucidated the mechanism underlying degradation of ERF1. Yeast two-hybrid screening showed that UBIQUITIN-CONJUGATING ENZYME 18 (UBC18) interacted with ERF1...
October 27, 2016: New Phytologist
https://www.readbyqxmd.com/read/27780814/plant-immunity-against-viruses-antiviral-immune-receptors-in-focus
#13
REVIEW
Iara P Calil, Elizabeth P B Fontes
BACKGROUND: Among the environmental limitations that affect plant growth, viruses cause major crop losses worldwide and represent serious threats to food security. Significant advances in the field of plant-virus interactions have led to an expansion of potential strategies for genetically engineered resistance in crops during recent years. Nevertheless, the evolution of viral virulence represents a constant challenge in agriculture that has led to a continuing interest in the molecular mechanisms of plant-virus interactions that affect disease or resistance...
October 24, 2016: Annals of Botany
https://www.readbyqxmd.com/read/27765354/anti-cancer-effect-of-epigallocatechin-3-gallate-egcg-in-head-and-neck-cancer-through-repression-of-transactivation-and-enhanced-degradation-of-%C3%AE-catenin
#14
Yoo Seob Shin, Sung Un Kang, Ju Kyeong Park, Yang Eun Kim, Yeon Soo Kim, Seung Joon Baek, Seong-Ho Lee, Chul-Ho Kim
BACKGROUND AND PURPOSE: Aberrant expression of β-catenin is highly associated with progression of various cancers including head and neck cancer (HNC). Green tea is most commonly used beverage in the world and one of the more bioactive compounds is the antioxidant epigallocatechin gallate (EGCG). This study was performed to investigate the mechanism by which EGCG inhibits the growth of HNC, focusing on the modulation of the expression and activity of β-catenin. METHODS: In vitro effects of EGCG on the transcription, translation, or degradation of β-catenin were investigated...
November 15, 2016: Phytomedicine: International Journal of Phytotherapy and Phytopharmacology
https://www.readbyqxmd.com/read/27730621/purification-of-26s-proteasomes-and-their-subcomplexes-from-plants
#15
Richard S Marshall, David C Gemperline, Richard D Vierstra
The 26S proteasome is a highly dynamic, multisubunit, ATP-dependent protease that plays a central role in cellular housekeeping and many aspects of plant growth and development by degrading aberrant polypeptides and key cellular regulators that are first modified by ubiquitin. Although the 26S proteasome was originally enriched from plants over 30 years ago, only recently have significant advances been made in our ability to isolate and study the plant particle. Here, we describe two robust methods for purifying the 26S proteasome and its subcomplexes from Arabidopsis thaliana; one that involves conventional chromatography techniques to isolate the complex from wild-type plants, and another that employs the genetic replacement of individual subunits with epitope-tagged variants combined with affinity purification...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/27726198/regulation-of-katanin-activity-in-the-ciliate-tetrahymena-thermophila
#16
Ewa Waclawek, Ewa Joachimiak, Malgorzata Hanna Hall, Hanna Fabczak, Dorota Wloga
Katanin is a microtubule severing protein that functions as a heterodimer composed of an AAA domain catalytic subunit, p60, and a regulatory subunit, a WD40 repeat protein, p80. Katanin-dependent severing of microtubules is important for proper execution of key cellular activities including cell division, migration, and differentiation. Published data obtained in Caenorhabditis elegans, Xenopus and mammals indicate that katanin is regulated at multiple levels including transcription, posttranslational modifications (of both katanin and microtubules) and degradation...
October 11, 2016: Molecular Microbiology
https://www.readbyqxmd.com/read/27704767/boc3arg-linked-ligands-induce-degradation-by-localizing-target-proteins-to-the-20s-proteasome
#17
Yuntao Shi, Marcus J C Long, Masha M Rosenberg, Shican Li, Aimee Kobjack, Philip Lessans, Rory T Coffey, Lizbeth Hedstrom
Targeted protein degradation is a promising strategy for drug design and functional assessment. Several small molecule approaches have been developed that localize target proteins to ubiquitin ligases, inducing ubiquitination and subsequent degradation by the 26S proteasome. We discovered that the degradation of a target protein can also be induced by a recognition ligand linked to tert-butyl carbamate (Boc3)-protected arginine (B3A). Here we show that this process requires the proteasome, but does not involve ubiquitination of the target protein...
October 5, 2016: ACS Chemical Biology
https://www.readbyqxmd.com/read/27676073/paraquat-tolerance3-is-an-e3-ligase-that-switches-off-activated-oxidative-response-by-targeting-histone-modifying-protein-methyltransferase4b
#18
Chao Luo, Xiao-Teng Cai, Jin Du, Tao-Lan Zhao, Peng-Fei Wang, Ping-Xia Zhao, Rui Liu, Qi Xie, Xiao-Feng Cao, Cheng-Bin Xiang
Oxidative stress is unavoidable for aerobic organisms. When abiotic and biotic stresses are encountered, oxidative damage could occur in cells. To avoid this damage, defense mechanisms must be timely and efficiently modulated. While the response to oxidative stress has been extensively studied in plants, little is known about how the activated response is switched off when oxidative stress is diminished. By studying Arabidopsis mutant paraquat tolerance3, we identified the genetic locus PARAQUAT TOLERANCE3 (PQT3) as a major negative regulator of oxidative stress tolerance...
September 2016: PLoS Genetics
https://www.readbyqxmd.com/read/27671749/arachidonic-acid-mediates-the-formation-of-abundant-alpha-helical-multimers-of-alpha-synuclein
#19
Marija Iljina, Laura Tosatto, Minee L Choi, Jason C Sang, Yu Ye, Craig D Hughes, Clare E Bryant, Sonia Gandhi, David Klenerman
The protein alpha-synuclein (αS) self-assembles into toxic beta-sheet aggregates in Parkinson's disease, while it is proposed that αS forms soluble alpha-helical multimers in healthy neurons. Here, we have made αS multimers in vitro using arachidonic acid (ARA), one of the most abundant fatty acids in the brain, and characterized them by a combination of bulk experiments and single-molecule Fӧrster resonance energy transfer (sm-FRET) measurements. The data suggest that ARA-induced oligomers are alpha-helical, resistant to fibril formation, more prone to disaggregation, enzymatic digestion and degradation by the 26S proteasome, and lead to lower neuronal damage and reduced activation of microglia compared to the oligomers formed in the absence of ARA...
September 27, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27668608/-inhibition-of-the-expression-of-proteasomal-genes-saccharomyces-cerevisiae-by-artificial-transcriptional-repressor
#20
B M Kirilenko, E N Grineva, D S Karpov, V L Karpov
26S proteasome is an ATP-dependent protease complex that takes part in cell homeostasis maintenance by the selective degradation of regulatory and damaged proteins. The proteasomal genes expression in Saccharomyces cerevisiae yeast is coordinately regulated by the system, which consists of the Rpn4 transcription factor and its binding site, called PACE. The ability to modulate proteasomal activity by changing the expression of its genes is an essential tool that can be used in fundamental studies devoted to the mechanisms of proteasome dependent cell processes, as well as in applied research for developing strategies to correct proteasome activity in some pathological processes...
July 2016: Molekuliarnaia Biologiia
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