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https://www.readbyqxmd.com/read/28324352/the-six-tomato-yellow-leaf-curl-virus-genes-expressed-individually-in-tomato-induce-different-levels-of-plant-stress-response-attenuation
#1
Rena Gorovits, Adi Moshe, Linoy Amrani, Rotem Kleinberger, Ghandi Anfoka, Henryk Czosnek
Tomato yellow leaf curl virus (TYLCV) is a begomovirus infecting tomato plants worldwide. TYLCV needs a healthy host environment to ensure a successful infection cycle for long periods. Hence, TYLCV restrains its destructive effect and induces neither a hypersensitive response nor cell death in infected tomatoes. On the contrary, TYLCV counteracts cell death induced by other factors, such as inactivation of HSP90 functionality. Suppression of plant death is associated with the inhibition of the ubiquitin 26S proteasome degradation and with a deactivation of the heat shock transcription factor HSFA2 pathways (including decreased HSP17 levels)...
March 21, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28292943/molecular-details-underlying-dynamic-structures-and-regulation-of-the-human-26s-proteasome
#2
Xiaorong Wang, Peter Cimermancic, Clinton Yu, Andreas Schweitzer, Nikita Chopra, James L Engel, Charles H Greenberg, Alexander S Huszagh, Florian Beck, Eri Sakata, Yingying Yang, Eric J Novitsky, Alexander Leitner, Paolo Nanni, Abdullah Kahraman, Xing Guo, Jack E Dixon, Scott D Rychnovsky, Ruedi Aebersold, Wolfgang Baumeister, Andrej Sali, Lan Huang
The 26S proteasome is the macromolecular machine responsible for ATP/ubiquitin dependent degradation. As aberration in proteasomal degradation has been implicated in many human diseases, structural analysis of the human 26S proteasome complex is essential to advance our understanding of its action and regulation mechanisms. In recent years, cross-linking mass spectrometry (XL-MS) has emerged as a powerful tool for elucidating structural topologies of large protein assemblies, with its unique capability of studying protein complexes in cells...
March 14, 2017: Molecular & Cellular Proteomics: MCP
https://www.readbyqxmd.com/read/28292892/noncanonical-role-of-arabidopsis-cop1-spa-complex-in-repressing-bin2-mediated-pif3-phosphorylation-and-degradation-in-darkness
#3
Jun-Jie Ling, Jian Li, Danmeng Zhu, Xing Wang Deng
The E3 ligase CONSTITUTIVELY PHOTOMORPHOGENIC 1 (COP1) has been known to mediate key signaling factors for degradation via the ubiquitin/26S proteasome pathway in both plants and animals. Here, we report a noncanonical function of Arabidopsis COP1, the central repressor of photomorphogenesis, in the form of a COP1/ SUPPRESSOR of phyA-105 (SPA) complex. We show that the COP1/SPA complex associates with and stabilizes PHYTOCHROME INTERACTING FACTOR 3 (PIF3) to repress photomorphogenesis in the dark. We identify the GSK3-like kinase BRASSINOSTEROID-INSENSITIVE 2 (BIN2) as a kinase of PIF3, which induces PIF3 degradation via 26S proteasome during skotomorphogenesis...
March 14, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28271482/cullin-ring-e3-ubiquitin-ligases-bridges-to-destruction
#4
Henry C Nguyen, Wei Wang, Yong Xiong
Ubiquitination is a highly conserved post-translational modification in eukaryotes, well known for targeting proteins for degradation by the 26S proteasome. Proteins destined for proteasomal degradation are selected by E3 ubiquitin ligases. Cullin-RING E3 ubiquitin ligases (CRLs) are the largest superfamily of E3 ubiquitin ligases, with over 400 members known in mammals. These modular complexes are tightly regulated in the cell. In this chapter, we highlight recent structural and biochemical advances shedding light on the assembly and architecture of cullin-RING ligases, their dynamic regulation by a variety of host factors, and their manipulation by viral pathogens and small molecules...
2017: Sub-cellular Biochemistry
https://www.readbyqxmd.com/read/28263418/crystal-structure-of-human-proteasome-assembly-chaperone-pac4-involved-in-proteasome-formation
#5
Eiji Kurimoto, Tadashi Satoh, Yuri Ito, Eri Ishihara, Kenta Okamoto, Maho Yagi-Utsumi, Keiji Tanaka, Koichi Kato
The 26S proteasome is a large protein complex, responsible for degradation of ubiquinated proteins in eukaryotic cells. Eukaryotic proteasome formation is a highly ordered process that is assisted by several assembly chaperones. The assembly of its catalytic 20S core particle depends on at least five proteasome-specific chaperones, i.e., proteasome-assembling chaperons 1-4 (PAC1-4) and proteasome maturation protein (POMP). The orthologues of yeast assembly chaperones have been structurally characterized, whereas most mammalian assembly chaperones are not...
March 6, 2017: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/28258412/reversible-phosphorylation-of-the-26s-proteasome
#6
REVIEW
Xing Guo, Xiuliang Huang, Mark J Chen
The 26S proteasome at the center of the ubiquitin-proteasome system (UPS) is essential for virtually all cellular processes of eukaryotes. A common misconception about the proteasome is that, once made, it remains as a static and uniform complex with spontaneous and constitutive activity for protein degradation. Recent discoveries have provided compelling evidence to support the exact opposite insomuch as the 26S proteasome undergoes dynamic and reversible phosphorylation under a variety of physiopathological conditions...
March 3, 2017: Protein & Cell
https://www.readbyqxmd.com/read/28254780/osftip1-mediated-regulation-of-florigen-transport-in-rice-is-negatively-regulated-by-a-ubiquitin-like-domain-kinase-osubdk%C3%AE-4
#7
Shiyong Song, Ying Chen, Lu Liu, Yanwen Wang, Shengjie Bao, Xuan Zhou, Zhi Wei Norman Teo, Chuanzao Mao, Yinbo Gan, Hao Yu
Flowering time is a critical agronomic trait that determines successful seed production and adaptation of crop plants. Photoperiodic control of this process in flowering plants is mediated by the long-distance mobile signal called florigen partly encoded by FLOWERING LOCUS T (FT) in Arabidopsis and its orthologs in other plant species. Despite the progress in understanding FT transport in the dicot model Arabidopsis, the mechanisms of florigen transport in monocots, which provide most of the biomass in agriculture, are unknown...
March 2, 2017: Plant Cell
https://www.readbyqxmd.com/read/28243125/carfilzomib-boosted-combination-therapy-for-relapsed-multiple-myeloma
#8
REVIEW
Raphael E Steiner, Elisabet E Manasanch
Carfilzomib is a proteasome inhibitor that binds selectively and irreversibly to the 20S proteasome, the proteolytic core particle within the 26S proteasome, resulting in the accumulation of proteasome substrates and ultimately growth arrest and apoptosis of tumor cells. The development and ultimate approval of this medication by regulatory agencies has been an important step toward improving clinical outcomes in multiple myeloma. Although initially approved as a single agent for the treatment of multiply relapsed and/or refractory myeloma, in the USA, it is now widely used in the early relapse setting in combination with lenalidomide and dexamethasone...
2017: OncoTargets and Therapy
https://www.readbyqxmd.com/read/28242843/label-free-proteomic-analysis-of-exosomes-derived-from-inducible-hepatitis-b-virus-replicating-hepad38-cell-line
#9
Xiaofang Jia, Jieliang Chen, Dominik A Megger, Xiaonan Zhang, Maya Kozlowski, Lijun Zhang, Zhong Fang, Jin Li, Qiaofang Chu, Min Wu, Yaming Li, Barbara Sitek, Zhenghong Yuan
Hepatitis B virus (HBV) infection is a major health problem worldwide. Recent evidence suggests that some viruses can manipulate the infection process by packing specific viral and cellular components into exosomes, small nanometer-sized (30-150 nm) vesicles secreted from various cells. However, the impact of HBV replication on the content of exosomes produced by hepatocytes has not been fully delineated. In this work, an HBV-inducible cell line HepAD38 was used to directly compare changes in the protein content of exosomes secreted from HepAD38 cells with or without HBV replication...
February 27, 2017: Molecular & Cellular Proteomics: MCP
https://www.readbyqxmd.com/read/28220418/in-vitro-ubiquitination-activity-assays-in-plant-immune-responses
#10
Giulia Furlan, Marco Trujillo
Ubiquitination is a central posttranslational modification that impinges on the fate of proteins. While attachment of K48-linked chains onto soluble proteins marks them for proteolysis via the 26S proteasome, mono-ubiquitination or K63-linked chains result in the endocytosis and sorting through the endomembrane system of integral membrane proteins, such as pattern recognition receptors. In vitro ubiquitination assays allow the biochemical analysis of all individual components of the ubiquitination machinery and its potential substrates...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28186089/adenovirus-mediated-tipe2-overexpression-inhibits-gastric-cancer-metastasis-via-reversal-of-epithelial-mesenchymal-transition
#11
H Yin, X Huang, M Tao, Q Hu, J Qiu, W Chen, J Wu, Y Xie
Tumor necrosis factor (TNF)-alpha-induced protein 8-like 2 (TNFAIP8L2; also termed TIPE2) has been shown to be involved in both the immune-negative modulation and cancer. We previously found that TIPE2 is lost in human gastric cancer, and TIPE2 restoration suppresses gastric cancer growth by induction of apoptosis and impairment of protein kinase B (PKB/AKT) and extracellular signal-regulated kinase-1/2 (ERK1/2) signaling. However, its correlation with epithelial-mesenchymal transition (EMT) in gastric cancer is largely elusive...
February 10, 2017: Cancer Gene Therapy
https://www.readbyqxmd.com/read/28184010/the-pepper-ring-type-e3-ligase-caairf1-regulates-the-aba-and-drought-signaling-via-caadip1-protein-phosphatase-degradation
#12
Chae Woo Lim, Woonhee Baek, Sung Chul Lee
Ubiquitin-mediated protein modification occurs at multiple steps of abscisic acid (ABA) signaling. Here, we sought proteins responsible for degradation of the pepper type 2C protein phosphatase CaADIP1 via the 26S proteasome system. We showed that the RING type E3 ligase CaAIRF1 (Capsicum annuum ADIP1 Interacting RING Finger Protein 1) interacts with and ubiquitinates CaADIP1. CaADIP1 degradation was slower in crude proteins from CaAIRF1-silenced peppers than in those from control plants. CaAIRF1-silenced pepper plants displayed reduced ABA sensitivity and decreased drought tolerance characterized by delayed stomatal closure and suppressed induction of ABA- and drought-responsive marker genes...
February 9, 2017: Plant Physiology
https://www.readbyqxmd.com/read/28168848/ora59-and-ein3-interaction-couples-jasmonate-ethylene-synergistic-action-to-antagonistic-salicylic-acid-regulation-of-pdf-expression
#13
Xiang He, Jishan Jiang, Changquan Wang, Katayoon Dehesh
Hormonal crosstalk is central for tailoring plant responses to the nature of challenges encountered. The role of antagonism between the two major defense hormones, salicylic acid (SA) and jasmonic acid (JA), and modulation of this interplay by ethylene (ET) in favor of JA signaling pathway in plant stress responses is well recognized, but the underlying mechanism is not fully understood. Here, we show the opposing function of two transcription factors, ethylene insensitive3 (EIN3) and EIN3-Like1 (EIL1), in SA-mediated suppression and JA-mediated activation of PLANT DEFENSIN1...
February 7, 2017: Journal of Integrative Plant Biology
https://www.readbyqxmd.com/read/28167764/hy5-a-positive-regulator-of-light-signaling-negatively-controls-the-unfolded-protein-response-in-arabidopsis
#14
Ganesh M Nawkar, Chang Ho Kang, Punyakishore Maibam, Joung Hun Park, Young Jun Jung, Ho Byoung Chae, Yong Hun Chi, In Jung Jung, Woe Yeon Kim, Dae-Jin Yun, Sang Yeol Lee
Light influences essentially all aspects of plant growth and development. Integration of light signaling with different stress response results in improvement of plant survival rates in ever changing environmental conditions. Diverse environmental stresses affect the protein-folding capacity of the endoplasmic reticulum (ER), thus evoking ER stress in plants. Consequently, the unfolded protein response (UPR), in which a set of molecular chaperones is expressed, is initiated in the ER to alleviate this stress...
February 6, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28159894/the-evolving-role-of-ubiquitin-modification-in-endoplasmic-reticulum-associated-degradation
#15
REVIEW
G Michael Preston, Jeffrey L Brodsky
The endoplasmic reticulum (ER) serves as a warehouse for factors that augment and control the biogenesis of nascent proteins entering the secretory pathway. In turn, this compartment also harbors the machinery that responds to the presence of misfolded proteins by targeting them for proteolysis via a process known as ER-associated degradation (ERAD). During ERAD, substrates are selected, modified with ubiquitin, removed from the ER, and then degraded by the cytoplasmic 26S proteasome. While integral membrane proteins can directly access the ubiquitination machinery that resides in the cytoplasm or on the cytoplasmic face of the ER membrane, soluble ERAD substrates within the lumen must be retrotranslocated from this compartment...
February 15, 2017: Biochemical Journal
https://www.readbyqxmd.com/read/28132691/de-novo-disruption-of-the-proteasome-regulatory-subunit-psmd12-causes-a-syndromic-neurodevelopmental-disorder
#16
Sébastien Küry, Thomas Besnard, Frédéric Ebstein, Tahir N Khan, Tomasz Gambin, Jessica Douglas, Carlos A Bacino, Stephan J Sanders, Andrea Lehmann, Xénia Latypova, Kamal Khan, Mathilde Pacault, Stephanie Sacharow, Kimberly Glaser, Eric Bieth, Laurence Perrin-Sabourin, Marie-Line Jacquemont, Megan T Cho, Elizabeth Roeder, Anne-Sophie Denommé-Pichon, Kristin G Monaghan, Bo Yuan, Fan Xia, Sylvain Simon, Dominique Bonneau, Philippe Parent, Brigitte Gilbert-Dussardier, Sylvie Odent, Annick Toutain, Laurent Pasquier, Deborah Barbouth, Chad A Shaw, Ankita Patel, Janice L Smith, Weimin Bi, Sébastien Schmitt, Wallid Deb, Mathilde Nizon, Sandra Mercier, Marie Vincent, Caroline Rooryck, Valérie Malan, Ignacio Briceño, Alberto Gómez, Kimberly M Nugent, James B Gibson, Benjamin Cogné, James R Lupski, Holly A F Stessman, Evan E Eichler, Kyle Retterer, Yaping Yang, Richard Redon, Nicholas Katsanis, Jill A Rosenfeld, Peter-Michael Kloetzel, Christelle Golzio, Stéphane Bézieau, Paweł Stankiewicz, Bertrand Isidor
Degradation of proteins by the ubiquitin-proteasome system (UPS) is an essential biological process in the development of eukaryotic organisms. Dysregulation of this mechanism leads to numerous human neurodegenerative or neurodevelopmental disorders. Through a multi-center collaboration, we identified six de novo genomic deletions and four de novo point mutations involving PSMD12, encoding the non-ATPase subunit PSMD12 (aka RPN5) of the 19S regulator of 26S proteasome complex, in unrelated individuals with intellectual disability, congenital malformations, ophthalmologic anomalies, feeding difficulties, deafness, and subtle dysmorphic facial features...
February 2, 2017: American Journal of Human Genetics
https://www.readbyqxmd.com/read/28121483/stress-induced-polyubiquitination-of-proteasomal-ubiquitin-receptors-targets-the-proteolytic-complex-for-autophagic-degradation
#17
Victoria Cohen-Kaplan, Aaron Ciechanover, Ido Livneh
Ubiquitin (Ub) is a small protein (8 kDa) found in all eukaryotic cells, which is conjugated covalently to numerous proteins, tagging them for recognition by a downstream effector. One of the best characterized functions of Ub is targeting proteins for either selective degradation by the proteasome, or for bulk degradation by the autophagy-lysosome system. The executing arm of the UPS is the 26S proteasome, a large multi-catalytic complex. While much is known about the synthesis and assembly of the proteasome's subunits, the mechanism(s) underlying its removal has remained obscure, similar to that of many other components of the ubiquitin-proteasome system...
January 25, 2017: Autophagy
https://www.readbyqxmd.com/read/28115689/structural-insights-into-the-functional-cycle-of-the-atpase-module-of-the-26s-proteasome
#18
Marc Wehmer, Till Rudack, Florian Beck, Antje Aufderheide, Günter Pfeifer, Jürgen M Plitzko, Friedrich Förster, Klaus Schulten, Wolfgang Baumeister, Eri Sakata
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)...
February 7, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28112451/calreticulin-is-a-fine-tuning-molecule-in-epibrassinolide-induced-apoptosis-through-activating-endoplasmic-reticulum-stress-in-colon-cancer-cells
#19
Pinar Obakan-Yerlikaya, Elif Damla Arisan, Ajda Coker-Gurkan, Kaan Adacan, Utku Özbey, Berna Somuncu, Didem Baran, Narçin Palavan-Ünsal
Epibrassinolide (EBR), a member of brassinostreoids plant hormones with cell proliferation promoting role in plants, is a natural polyhydroxysteroid with structural similarity to steroid hormones of vertebrates. EBR has antiproliferative and apoptosis-inducing effect in various cancer cells. Although EBR has been shown to affect survival and mitochondria-mediated apoptosis pathways in a p53-independent manner, the exact molecular targets of EBR are still under investigation. Our recent SILAC (Stable Isotope Labeling by Amino Acids in Cell Culture) data showed that the most significantly altered protein after EBR treatment was calreticulin (CALR)...
January 23, 2017: Molecular Carcinogenesis
https://www.readbyqxmd.com/read/28112445/calcium-dependent-protein-kinase-cpk28-targets-the-methionine-adenosyltransferases-for-degradation-by-the-26s-proteasome-and-affects-ethylene-biosynthesis-and-lignin-deposition-in-arabidopsis
#20
Yu Jin, Nenghui Ye, Fuyuan Zhu, Haoxuan Li, Juan Wang, Liwen Jiang, Jianhua Zhang
S-adenosylmethionine (AdoMet) is synthesized by methionine adenosyltransferase (MAT) and plays an essential role in ethylene biosynthesis and other methylation reactions. Despite increasing knowledge of MAT regulation at transcriptional levels, how MAT is post-translationally regulated remains unknown in plant cells. Phosphorylation is an important post-translational modification for regulating the activity of enzymes, protein function and signaling transduction. Using molecular and biochemical approaches, we have identified the phosphorylation of MAT proteins by calcium dependent protein kinase (CPK28)...
January 23, 2017: Plant Journal: for Cell and Molecular Biology
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