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https://www.readbyqxmd.com/read/28186089/adenovirus-mediated-tipe2-overexpression-inhibits-gastric-cancer-metastasis-via-reversal-of-epithelial-mesenchymal-transition
#1
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
#2
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
#3
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
#4
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
#5
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
#6
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
#7
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
#8
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
#9
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
#10
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
https://www.readbyqxmd.com/read/28106073/high-resolution-cryo-em-structure-of-the-proteasome-in-complex-with-adp-alfx
#11
Zhanyu Ding, Zhenglin Fu, Cong Xu, Yifan Wang, Yanxing Wang, Junrui Li, Liangliang Kong, Jinhuan Chen, Na Li, Rongguang Zhang, Yao Cong
The 26S proteasome is an ATP-dependent dynamic 2.5 MDa protease that regulates numerous essential cellular functions through degradation of ubiquitinated substrates. Here we present a near-atomic-resolution cryo-EM map of the S. cerevisiae 26S proteasome in complex with ADP-AlFx. Our biochemical and structural data reveal that the proteasome-ADP-AlFx is in an activated state, displaying a distinct conformational configuration especially in the AAA-ATPase motor region. Noteworthy, this map demonstrates an asymmetric nucleotide binding pattern with four consecutive AAA-ATPase subunits bound with nucleotide...
January 20, 2017: Cell Research
https://www.readbyqxmd.com/read/28104751/exercise-training-decreases-nadph-oxidase-activity-and-restores-skeletal-muscle-mass-in-heart-failure-rats
#12
Telma F Cunha, Luiz Roberto Grassman Bechara, Aline V N Bacurau, Paulo R Jannig, Vanessa Azevedo Voltarelli, Paulo M Dourado, Andrea R Vasconcelos, Cristóforo Scavone, Julio C B Ferreira, Patricia C Brum
We have recently demonstrated that NADPH oxidase hyperactivity, NF-κB activation and increased p38 phosphorylation lead to atrophy of glycolytic muscle in heart failure (HF). Aerobic exercise training (AET) is an efficient strategy to counteract skeletal muscle atrophy in this syndrome. Therefore, we tested whether AET would regulate muscle redox balance and protein degradation by decreasing NADPH oxidase hyperactivity, reestablishing NF-κB signaling, p38 phosphorylation and proteasome activity in plantaris muscle of myocardial infarcted-induced HF (MI) rats...
January 19, 2017: Journal of Applied Physiology
https://www.readbyqxmd.com/read/28100709/the-arabidopsis-ring-type-e3-ligase-tear1-controls-leaf-development-by-targeting-the-tie1-transcriptional-repressor-for-degradation
#13
Jinzhe Zhang, Baoye Wei, Rongrong Yuan, Jianhui Wang, Mingxin Ding, Zhuoyao Chen, Hao Yu, Genji Qin
The developmental plasticity of leaf size and shape is important for leaf function and plant survival. However, the mechanisms by which plants form diverse leaves in response to environmental conditions are not well understood. Here, we identified TIE1-ASSOCIATED RING-TYPE E3 LIGASE 1 (TEAR1), and found that it regulates leaf development by promoting the degradation of TCP INTERACTOR-CONTAINING EAR MOTIF PROTEIN 1 (TIE1), an important repressor of CINCINNATA (CIN)-like TEOSINTE BRANCHED1/CYCLOIDEA/PCF (TCP) transcription factors, which are key for leaf development...
January 18, 2017: Plant Cell
https://www.readbyqxmd.com/read/28088021/sanguinarine-induced-oxidative-stress-and-apoptosis-like-programmed-cell-death-al-pcd-in-root-meristem-cells-of-allium-cepa
#14
Aneta Żabka, Konrad Winnicki, Justyna Teresa Polit, Janusz Maszewski
A vast number of studies on plant cell systems clearly indicate that various biotic and abiotic stresses give rise to the uncontrolled increase in the level of reactive oxygen species (ROS). Excess concentrations of ROS result in damage to proteins, lipids, carbohydrates, and DNA, which may lead, in consequence, to the apoptotic cell death. The current study investigates the effects of sanguinarine (SAN), a natural alkaloid derived from the roots of Sanguinaria canadensis, on root apical meristem cells of Allium cepa...
January 4, 2017: Plant Physiology and Biochemistry: PPB
https://www.readbyqxmd.com/read/28077573/a-retrochaperone-function-for-cdc48-the-cdc48-complex-is-required-for-retrotranslocated-erad-m-substrate-solubility
#15
Sonya E Neal, Raymond Mak, Eric J Bennett, Randolph Hampton
A surprising feature of ER-associated degradation (ERAD) is the movement, or retrotranslocation, of ubiquitinated substrates from the ER lumen or membrane to the cytosol where they are degraded by the 26S proteasome. Multispanning ER membrane proteins, called ERAD-M substrates, are retrotranslocated to the cytosol as full-length intermediates during ERAD and we have investigated how they maintain solubility. Using an in vivo assay, we show that retrotranslocated ERAD-M substrates are moved to the cytoplasm as part of the normal ERAD pathway, where they are part of a solely proteinacious complex...
January 11, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28073696/spop-promotes-sirt2-degradation-and-suppresses-non-small-cell-lung-cancer-cell-growth
#16
Jie Luo, Yu-Chen Bao, Xian-Xiu Ji, Bin Chen, Qin-Fang Deng, Song-Wen Zhou
SIRT2 is a NAD-dependent deacetylase and inhibition of SIRT2 has a broad anticancer activity. Here we report that SPOP binds to SIRT2 and mediates its degradation by the 26S proteasome, which can be blocked by MG132 treatment. We also found that the levels of SPOP significantly decreased, while the levels of SIRT2 significantly increased in non-small cell lung cancer (NSCLC) cell lines, compared to normal bronchial epithelial cell line and NSCLC specimens, compared to the paired non-tumor lung tissue. Furthermore, SPOP can suppress NSCLC cell growth...
January 7, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28069863/ubiquitin-recognition-by-the-proteasome
#17
REVIEW
Yasushi Saeki
The 26S proteasome is a 2.5-MDa complex responsible for the selective, ATP-dependent degradation of ubiquitylated proteins in eukaryotic cells. Substrates in hundreds cellular pathways are timely ubiquitylated and converged to the proteasome by direct recognition or by multiple shuttle factors. Engagement of substrate protein triggers conformational changes of the proteasome, which drive substrate unfolding, deubiquitylation and translocation of substrates to proteolytic sites. Recent studies have challenged the previous paradigm that Lys48-linked tetraubiquitin is a minimal degradation signal: in addition, monoubiquitylation or multiple short ubiquitylations can serve as the targeting signal for proteasomal degradation...
January 8, 2017: Journal of Biochemistry
https://www.readbyqxmd.com/read/28059715/control-of-meiotic-pairing-and-recombination-by-chromosomally-tethered-26s-proteasome
#18
Jasvinder S Ahuja, Rima Sandhu, Rana Mainpal, Crystal Lawson, Hanna Henley, Patricia A Hunt, Judith L Yanowitz, G Valentin Börner
During meiosis, paired homologous chromosomes (homologs) become linked via the synaptonemal complex (SC) and crossovers. Crossovers mediate homolog segregation and arise from self-inflicted double-strand breaks (DSBs). Here, we identified a role for the proteasome, the multisubunit protease that degrades proteins in the nucleus and cytoplasm, in homolog juxtaposition and crossing over. Without proteasome function, homologs failed to pair and instead remained associated with nonhomologous chromosomes. Although dispensable for noncrossover formation, a functional proteasome was required for a coordinated transition that entails SC assembly between longitudinally organized chromosome axes and stable strand exchange of crossover-designated DSBs...
January 27, 2017: Science
https://www.readbyqxmd.com/read/28055010/continued-26s-proteasome-dysfunction-in-mouse-brain-cortical-neurons-impairs-autophagy-and-the-keap1-nrf2-oxidative-defence-pathway
#19
Aslihan Ugun-Klusek, Michael H Tatham, Jamal Elkharaz, Dumitru Constantin-Teodosiu, Karen Lawler, Hala Mohamed, Simon M L Paine, Glen Anderson, R John Mayer, James Lowe, E Ellen Billett, Lynn Bedford
The ubiquitin-proteasome system (UPS) and macroautophagy (autophagy) are central to normal proteostasis and interdependent in that autophagy is known to compensate for the UPS to alleviate ensuing proteotoxic stress that impairs cell function. UPS and autophagy dysfunctions are believed to have a major role in the pathomechanisms of neurodegenerative disease. Here we show that continued 26S proteasome dysfunction in mouse brain cortical neurons causes paranuclear accumulation of fragmented dysfunctional mitochondria, associated with earlier recruitment of Parkin and lysine 48-linked ubiquitination of mitochondrial outer membrane (MOM) proteins, including Mitofusin-2...
January 5, 2017: Cell Death & Disease
https://www.readbyqxmd.com/read/28013174/dwarf-and-short-grain-1-encoding-a-putative-u-box-protein-regulates-cell-division-and-elongation-in-rice
#20
Nan Wang, Yadi Xing, Qijin Lou, Ping Feng, Song Liu, Meidan Zhu, Wuzhong Yin, Shunran Fang, Yan Lin, Tianquan Zhang, Xianchun Sang, Guanghua He
Plant hormones coordinate a plant's responses to environmental stimuli and the endogenous developmental programs for cell division and elongation. Brassinosteroids are among the most important of these hormones in plant development. Recently, the ubiquitin-26S-proteasome system was identified to play a key role in hormone biology. In this study, we analyzed the function of a rice (Oryza sativa) gene, DSG1, which encodes a U-box E3 ubiquitin ligase. In the dsg1 mutant (an allelic mutant of tud1), the lengths of the roots, internodes, panicles, and seeds were shorter than that in the wild-type, which was due to defects in cell division and elongation...
December 7, 2016: Journal of Plant Physiology
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