Journal articles: 'Science induces'

1

Stajic, J. "Thinning films induces ferroelectricity." Science 349, no. 6254 (September 17, 2015): 1296–97. http://dx.doi.org/10.1126/science.349.6254.1296-e.

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Costantino, Lorenzo, Sotirios K. Sotiriou, Juha K. Rantala, Simon Magin, Emil Mladenov, Thomas Helleday, James E. Haber, George Iliakis, Olli P. Kallioniemi, and Thanos D. Halazonetis. "Break-Induced Replication Repair of Damaged Forks Induces Genomic Duplications in Human Cells." Science 343, no. 6166 (December 5, 2013): 88–91. http://dx.doi.org/10.1126/science.1243211.

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In budding yeast, one-ended DNA double-strand breaks (DSBs) and damaged replication forks are repaired by break-induced replication (BIR), a homologous recombination pathway that requires the Pol32 subunit of DNA polymerase delta. DNA replication stress is prevalent in cancer, but BIR has not been characterized in mammals. In a cyclin E overexpression model of DNA replication stress, POLD3, the human ortholog of POL32, was required for cell cycle progression and processive DNA synthesis. Segmental genomic duplications induced by cyclin E overexpression were also dependent on POLD3, as were BIR-mediated recombination events captured with a specialized DSB repair assay. We propose that BIR repairs damaged replication forks in mammals, accounting for the high frequency of genomic duplications in human cancers.

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Sugden, A. M. "ECOLOGY/EVOLUTION: Fishing Induces Regime Change." Science 317, no. 5834 (July 6, 2007): 18a. http://dx.doi.org/10.1126/science.317.5834.18a.

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4

Alderton, Gemma. "High caloric intake induces inflammation." Science 359, no. 6375 (February 1, 2018): 531.2–532. http://dx.doi.org/10.1126/science.359.6375.531-b.

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Meibom, K. L. "Chitin Induces Natural Competence in Vibrio cholerae." Science 310, no. 5755 (December 16, 2005): 1824–27. http://dx.doi.org/10.1126/science.1120096.

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Foley, John F. "IRF2 induces gasdermin D for pyroptosis." Science 364, no. 6442 (May 23, 2019): 746.18–748. http://dx.doi.org/10.1126/science.364.6442.746-r.

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Alderton, Gemma. "A new target induces synthetic lethality." Science 359, no. 6381 (March 15, 2018): 1227.18–1229. http://dx.doi.org/10.1126/science.359.6381.1227-r.

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Shi, C., and C. T. Murphy. "Mating Induces Shrinking and Death in Caenorhabditis Mothers." Science 343, no. 6170 (December 19, 2013): 536–40. http://dx.doi.org/10.1126/science.1242958.

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9

Whitlock, J. R. "Learning Induces Long-Term Potentiation in the Hippocampus." Science 313, no. 5790 (August 25, 2006): 1093–97. http://dx.doi.org/10.1126/science.1128134.

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Singh, S. B., A. S. Davis, G. A. Taylor, and V. Deretic. "Human IRGM Induces Autophagy to Eliminate Intracellular Mycobacteria." Science 313, no. 5792 (August 3, 2006): 1438–41. http://dx.doi.org/10.1126/science.1129577.

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Shirane, M., and K. I. Nakayama. "Protrudin Induces Neurite Formation by Directional Membrane Trafficking." Science 314, no. 5800 (November 3, 2006): 818–21. http://dx.doi.org/10.1126/science.1134027.

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12

Yu, X. J., K. McGourty, M. Liu, K. E. Unsworth, and D. W. Holden. "pH Sensing by Intracellular Salmonella Induces Effector Translocation." Science 328, no. 5981 (April 15, 2010): 1040–43. http://dx.doi.org/10.1126/science.1189000.

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13

Wootton, Sarah K., Christine L. Halbert, and A. Dusty Miller. "Envelope Proteins of Jaagsiekte Sheep Retrovirus and Enzootic Nasal Tumor Virus Induce Similar Bronchioalveolar Tumors in Lungs of Mice." Journal of Virology 80, no. 18 (September 15, 2006): 9322–25. http://dx.doi.org/10.1128/jvi.00865-06.

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ABSTRACT Jaagsiekte sheep retrovirus (JSRV) induces bronchioalveolar tumors in sheep and goats. Expression of the JSRV envelope (Env) protein in mouse airway epithelial cells induces similar tumors, indicating that Env expression is sufficient for tissue-specific tumor formation. Enzootic nasal tumor virus (ENTV) is related to JSRV but induces tumors in the nasal epithelium of sheep and goats. Here we found that ENTV Env can also induce tumors in mice but, unexpectedly, with a phenotype identical to that of tumors induced by the JSRV Env, indicating that factors other than Env mediate the tissue specificity of tumor induction by ENTV.

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14

Evans, James A. "Industry Induces Academic Science to Know Less about More." American Journal of Sociology 116, no. 2 (September 2010): 389–452. http://dx.doi.org/10.1086/653834.

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15

Greenberg, M., E. Ziff, and L. Greene. "Stimulation of neuronal acetylcholine receptors induces rapid gene transcription." Science 234, no. 4772 (October 3, 1986): 80–83. http://dx.doi.org/10.1126/science.3749894.

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16

Rao, M. "Transmembrane Protein GDE2 Induces Motor Neuron Differentiation in Vivo." Science 309, no. 5744 (September 30, 2005): 2212–15. http://dx.doi.org/10.1126/science.1117156.

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17

Blackstone, E. "H2S Induces a Suspended Animation-Like State in Mice." Science 308, no. 5721 (April 22, 2005): 518. http://dx.doi.org/10.1126/science.1108581.

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18

Takano, Kazunori, Haruko Watanabe-Takano, Shiro Suetsugu, Souichi Kurita, Kazuya Tsujita, Sumiko Kimura, Takashi Karatsu, Tadaomi Takenawa, and Takeshi Endo. "Nebulin and N-WASP Cooperate to Cause IGF-1–Induced Sarcomeric Actin Filament Formation." Science 330, no. 6010 (December 9, 2010): 1536–40. http://dx.doi.org/10.1126/science.1197767.

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Insulin-like growth factor 1 (IGF-1) induces skeletal muscle maturation and enlargement (hypertrophy). These responses require protein synthesis and myofibril formation (myofibrillogenesis). However, the signaling mechanisms of myofibrillogenesis remain obscure. We found that IGF-1–induced phosphatidylinositol 3-kinase–Akt signaling formed a complex of nebulin and N-WASP at the Z bands of myofibrils by interfering with glycogen synthase kinase-3β in mice. Although N-WASP is known to be an activator of the Arp2/3 complex to form branched actin filaments, the nebulin–N-WASP complex caused actin nucleation for unbranched actin filament formation from the Z bands without the Arp2/3 complex. Furthermore, N-WASP was required for IGF-1–induced muscle hypertrophy. These findings present the mechanisms of IGF-1–induced actin filament formation in myofibrillogenesis required for muscle maturation and hypertrophy and a mechanism of actin nucleation.

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19

Worthen, G., B. Schwab, E. Elson, and G. Downey. "Mechanics of stimulated neutrophils: cell stiffening induces retention in capillaries." Science 245, no. 4914 (July 14, 1989): 183–86. http://dx.doi.org/10.1126/science.2749255.

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20

Wilkins, Bryan J., Nils A. Rall, Yogesh Ostwal, Tom Kruitwagen, Kyoko Hiragami-Hamada, Marco Winkler, Yves Barral, Wolfgang Fischle, and Heinz Neumann. "A Cascade of Histone Modifications Induces Chromatin Condensation in Mitosis." Science 343, no. 6166 (January 2, 2014): 77–80. http://dx.doi.org/10.1126/science.1244508.

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Metaphase chromosomes are visible hallmarks of mitosis, yet our understanding of their structure and of the forces shaping them is rudimentary. Phosphorylation of histone H3 serine 10 (H3 S10) by Aurora B kinase is a signature event of mitosis, but its function in chromatin condensation is unclear. Using genetically encoded ultraviolet light-inducible cross-linkers, we monitored protein-protein interactions with spatiotemporal resolution in living yeast to identify the molecular details of the pathway downstream of H3 S10 phosphorylation. This modification leads to the recruitment of the histone deacetylase Hst2p that subsequently removes an acetyl group from histone H4 lysine 16, freeing the H4 tail to interact with the surface of neighboring nucleosomes and promoting fiber condensation. This cascade of events provides a condensin-independent driving force of chromatin hypercondensation during mitosis.

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21

Helaine, S., A. M. Cheverton, K. G. Watson, L. M. Faure, S. A. Matthews, and D. W. Holden. "Internalization of Salmonella by Macrophages Induces Formation of Nonreplicating Persisters." Science 343, no. 6167 (January 9, 2014): 204–8. http://dx.doi.org/10.1126/science.1244705.

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22

Prudhomme, Marc, Laetitia Attaiech, Guillaume Sanchez, Bernard Martin, and Jean-Pierre Claverys. "Antibiotic Stress Induces Genetic Transformability in the Human PathogenStreptococcus pneumoniae." Science 313, no. 5783 (July 7, 2006): 89–92. http://dx.doi.org/10.1126/science.1127912.

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23

Bilic, J., Y. L. Huang, G. Davidson, T. Zimmermann, C. M. Cruciat, M. Bienz, and C. Niehrs. "Wnt Induces LRP6 Signalosomes and Promotes Dishevelled-Dependent LRP6 Phosphorylation." Science 316, no. 5831 (June 15, 2007): 1619–22. http://dx.doi.org/10.1126/science.1137065.

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24

Egan, S., J. Wright, L. Jarolim, K. Yanagihara, R. Bassin, and A. Greenberg. "Transformation by oncogenes encoding protein kinases induces the metastatic phenotype." Science 238, no. 4824 (October 9, 1987): 202–5. http://dx.doi.org/10.1126/science.3659911.

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25

Hill, T., N. Dean, and A. Boynton. "Inositol 1,3,4,5-tetrakisphosphate induces Ca2+ sequestration in rat liver cells." Science 242, no. 4882 (November 25, 1988): 1176–78. http://dx.doi.org/10.1126/science.2847317.

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26

Jaglo-Ottosen, K. R. "Arabidopsis CBF1 Overexpression Induces COR Genes and Enhances Freezing Tolerance." Science 280, no. 5360 (April 3, 1998): 104–6. http://dx.doi.org/10.1126/science.280.5360.104.

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27

Nougayrede, J. P. "Escherichia coli Induces DNA Double-Strand Breaks in Eukaryotic Cells." Science 313, no. 5788 (August 11, 2006): 848–51. http://dx.doi.org/10.1126/science.1127059.

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28

Kašparovský, T., M. L. Milat, J. P. Blein, L. Havel, and V. Mikeš. "Ergosterol induces mobilization of internal calcium in tobacco cells." Plant Protection Science 38, SI 2 - 6th Conf EFPP 2002 (December 31, 2017): 516–18. http://dx.doi.org/10.17221/10542-pps.

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As for natural sterols, only ergosterol is recognized very specifically and sensitively (nM) by plants cells. Ergosterol interacts with tobacco suspension cells and trigger pH changes of extracellular medium, oxidative burst and synthesis of phytoalexins. Compared with the responses induced by cryptogein, a proteinaceous elicitor from Phytophthora sp., oxidative burst, DpH and phytoalexin accumulation were weaker with ergosterol. Cryptogein stimulated an apparent continuous uptake of external calcium within 40 min, whereas no net uptake of external calcium occurred upon the addition of ergosterol. However, the elicitation with either cryptogein or ergosterol resulted in an increase of the fluorescence of calcium green 1 in cytosol. The use of several inhibitors of calcium channels (La<sup>3+</sup>, TMB-8, verapamil, ruthenium red, nifedipine) and a protein-kinase inhibitors (staurosporin, NPC-15437, H-89) suggests that the elicitation with ergosterol includes the mobilization of internal calcium stores in vacuoles mediated by IP3 and some protein kinases.

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29

Catania, Kenneth. "The shocking predatory strike of the electric eel." Science 346, no. 6214 (December 4, 2014): 1231–34. http://dx.doi.org/10.1126/science.1260807.

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Electric eels can incapacitate prey with an electric discharge, but the mechanism of the eel’s attack is unknown. Through a series of experiments, I show that eel high-voltage discharges can activate prey motor neurons, and hence muscles, allowing eels to remotely control their target. Eels prevent escape in free-swimming prey using high-frequency volleys to induce immobilizing whole-body muscle contraction (tetanus). Further, when prey are hidden, eels can emit periodic volleys of two or three discharges that cause massive involuntary twitch, revealing the prey’s location and eliciting the full, tetanus-inducing volley. The temporal patterns of eel electrical discharges resemble motor neuron activity that induces fast muscle contraction, suggesting that eel high-voltage volleys have been selected to most efficiently induce involuntary muscle contraction in nearby animals.

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30

Cohen, Y. "Systemic induced resistance." Plant Protection Science 38, SI 1 - 6th Conf EFPP 2002 (January 1, 2002): S122—S125. http://dx.doi.org/10.17221/10334-pps.

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Biotic and abiotic agents may induce resistance in plants against pathogens. Abiotic agents may be synthetic or natural. The natural, non-protein amino acid BABA (DL-β-aminobutyric acid) induces systemic resistance in crop plants against pathogens. Dry, killed mycelia of Penicillium chrysogenum (DM) induces local resistance in plants against soil-borne pathogens. The activity of BABA and DM are described here in detail. Both products were shown to effectively control plant disease in nature.

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31

Darius, H., DJ Lefer, JB Smith, and AM Lefer. "Role of platelet-activating factor-acether in mediating guinea pig anaphylaxis." Science 232, no. 4746 (April 4, 1986): 58–60. http://dx.doi.org/10.1126/science.3082008.

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The pathophysiology of anaphylaxis is very complex, and the sequelae of events are not fully explained in terms of the effects of histamine and peptide leukotrienes alone. Platelet-activating factor (1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine, PAF-acether) has been detected in animals undergoing anaphylaxis. Injection of synthetic PAF-acether induces similar effects, including bronchoconstriction, respiratory arrest, systemic hypotension, neutropenia, and thrombocytopenia. The results reported here demonstrate that the histamine- and leukotriene-independent component of guinea pig anaphylaxis in vivo and in isolated lung parenchymal strips in vitro is mediated by PAF-acether. However, PAF-acether is not responsible for the anaphylaxis-induced thrombocytopenia.

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32

Morita, Eiji, Akitoshi Nakashima, Hironobu Asao, Hiroyuki Sato, and Kazuo Sugamura. "Human Parvovirus B19 Nonstructural Protein (NS1) Induces Cell Cycle Arrest at G1 Phase." Journal of Virology 77, no. 5 (March 1, 2003): 2915–21. http://dx.doi.org/10.1128/jvi.77.5.2915-2921.2003.

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ABSTRACT Human parvovirus B19 infects predominantly erythroid precursor cells, leading to inhibition of erythropoiesis. This erythroid cell damage is mediated by the viral nonstructural protein 1 (NS1) through an apoptotic mechanism. We previously demonstrated that B19 virus infection induces G2 arrest in erythroid UT7/Epo-S1 cells; however, the role of NS1 in regulating cell cycle arrest is unknown. In this report, by using paclitaxel, a mitotic inhibitor, we show that B19 virus infection induces not only G2 arrest but also G1 arrest. Interestingly, UV-irradiated B19 virus, which has inactivated the expression of NS1, still harbors the ability to induce G2 arrest but not G1 arrest. Furthermore, treatment with caffeine, a G2 checkpoint inhibitor, abrogated the B19 virus-induced G2 arrest despite expression of NS1. These results suggest that the B19 virus-induced G2 arrest is not mediated by NS1 expression. We also found that NS1-transfected UT7/Epo-S1 and 293T cells induced cell cycle arrest at the G1 phase. These results indicate that NS1 expression plays a critical role in G1 arrest induced by B19 virus. Furthermore, NS1 expression significantly increased p21/WAF1 expression, a cyclin-dependent kinase inhibitor that induces G1 arrest. Thus, G1 arrest mediated by NS1 may be a prerequisite for the apoptotic damage of erythroid progenitor cells upon B19 virus infection.

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33

Suzumura, A., E. Lavi, Weiss, and D. Silberberg. "Coronavirus infection induces H-2 antigen expression on oligodendrocytes and astrocytes." Science 232, no. 4753 (May 23, 1986): 991–93. http://dx.doi.org/10.1126/science.3010460.

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34

Hand, T. W., L. M. Dos Santos, N. Bouladoux, M. J. Molloy, A. J. Pagan, M. Pepper, C. L. Maynard, C. O. Elson, and Y. Belkaid. "Acute Gastrointestinal Infection Induces Long-Lived Microbiota-Specific T Cell Responses." Science 337, no. 6101 (August 23, 2012): 1553–56. http://dx.doi.org/10.1126/science.1220961.

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35

Wang, F., J. Travins, B. DeLaBarre, V. Penard-Lacronique, S. Schalm, E. Hansen, K. Straley, et al. "Targeted Inhibition of Mutant IDH2 in Leukemia Cells Induces Cellular Differentiation." Science 340, no. 6132 (April 4, 2013): 622–26. http://dx.doi.org/10.1126/science.1234769.

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36

Bian, G., D. Joshi, Y. Dong, P. Lu, G. Zhou, X. Pan, Y. Xu, G. Dimopoulos, and Z. Xi. "Wolbachia Invades Anopheles stephensi Populations and Induces Refractoriness to Plasmodium Infection." Science 340, no. 6133 (May 9, 2013): 748–51. http://dx.doi.org/10.1126/science.1236192.

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37

Peters, N., J. Frost, and S. Long. "A plant flavone, luteolin, induces expression of Rhizobium meliloti nodulation genes." Science 233, no. 4767 (August 29, 1986): 977–80. http://dx.doi.org/10.1126/science.3738520.

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38

Cornell-Bell, A., S. Finkbeiner, M. Cooper, and S. Smith. "Glutamate induces calcium waves in cultured astrocytes: long-range glial signaling." Science 247, no. 4941 (January 26, 1990): 470–73. http://dx.doi.org/10.1126/science.1967852.

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39

Sommers, C. L. "A LAT Mutation That Inhibits T Cell Development Yet Induces Lymphoproliferation." Science 296, no. 5575 (June 14, 2002): 2040–43. http://dx.doi.org/10.1126/science.1069066.

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40

Premi, S., S. Wallisch, C. M. Mano, A. B. Weiner, A. Bacchiocchi, K. Wakamatsu, E. J. H. Bechara, R. Halaban, T. Douki, and D. E. Brash. "Chemiexcitation of melanin derivatives induces DNA photoproducts long after UV exposure." Science 347, no. 6224 (February 19, 2015): 842–47. http://dx.doi.org/10.1126/science.1256022.

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41

PEARCE, G., D. STRYDOM, S. JOHNSON, and C. A. RYAN. "A Polypeptide from Tomato Leaves Induces Wound-Inducible Proteinase Inhibitor Proteins." Science 253, no. 5022 (August 23, 1991): 895–97. http://dx.doi.org/10.1126/science.253.5022.895.

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42

Manuelidis, Laura, William Fritch, and You-Gen Xi. "Evolution of a Strain of CJD That Induces BSE-Like Plaques." Science 277, no. 5322 (July 4, 1997): 94–98. http://dx.doi.org/10.1126/science.277.5322.94.

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43

Seo, J. Y., R. Yaneva, E. R. Hinson, and P. Cresswell. "Human Cytomegalovirus Directly Induces the Antiviral Protein Viperin to Enhance Infectivity." Science 332, no. 6033 (April 28, 2011): 1093–97. http://dx.doi.org/10.1126/science.1202007.

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44

Zurawski, G., M. Benedik, B. Kamb, J. Abrams, S. Zurawski, and F. Lee. "Activation of mouse T-helper cells induces abundant preproenkephalin mRNA synthesis." Science 232, no. 4751 (May 9, 1986): 772–75. http://dx.doi.org/10.1126/science.2938259.

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45

Syassen, N., D. M. Bauer, M. Lettner, T. Volz, D. Dietze, J. J. Garcia-Ripoll, J. I. Cirac, G. Rempe, and S. Durr. "Strong Dissipation Inhibits Losses and Induces Correlations in Cold Molecular Gases." Science 320, no. 5881 (June 6, 2008): 1329–31. http://dx.doi.org/10.1126/science.1155309.

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46

Goto, Yukihisa, Noriko Maki, Yasunori Ichihashi, Daisuke Kitazawa, Daisuke Igarashi, Yasuhiro Kadota, and Ken Shirasu. "Exogenous Treatment with Glutamate Induces Immune Responses in Arabidopsis." Molecular Plant-Microbe Interactions® 33, no. 3 (March 2020): 474–87. http://dx.doi.org/10.1094/mpmi-09-19-0262-r.

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Plant resistance inducers (PRIs) are compounds that protect plants from diseases by activating immunity responses. Exogenous treatment with glutamate (Glu), an important amino acid for all living organisms, induces resistance against fungal pathogens in rice and tomato. To understand the molecular mechanisms of Glu-induced immunity, we used the Arabidopsis model system. We found that exogenous treatment with Glu induces resistance against pathogens in Arabidopsis. Consistent with this, transcriptome analyses of Arabidopsis seedlings showed that Glu significantly induces the expression of wound-, defense-, and stress-related genes. Interestingly, Glu activates the expression of genes induced by pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns at much later time points than the flg22 peptide, which is a bacterial-derived PAMP. The Glu receptor-like (GLR) proteins GLR3.3 and GLR3.6 are involved in the early expression of Glu-inducible genes; however, the sustained expression of these genes does not require the GLR proteins. Glu-inducible gene expression is also not affected by mutations in genes that encode PAMP receptors (EFR, FLS2, and CERK1), regulators of pattern-triggered immunity (BAK1, BKK1, BIK1, and PBL1), or a salicylic acid biosynthesis enzyme (SID2). The treatment of roots with Glu activates the expression of PAMP-, salicylic acid-, and jasmonic acid-inducible genes in leaves. Moreover, the treatment of roots with Glu primes chitin-induced responses in leaves, possibly through transcriptional activation of LYSIN-MOTIF RECEPTOR-LIKE KINASE 5 (LYK5), which encodes a chitin receptor. Because Glu treatment does not cause discernible growth retardation, Glu can be used as an effective PRI.

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47

Ruvolo, Vivian, Lorena Navarro, Clare E. Sample, Michael David, Seung Sung, and Sankar Swaminathan. "The Epstein-Barr Virus SM Protein Induces STAT1 and Interferon-Stimulated Gene Expression." Journal of Virology 77, no. 6 (March 15, 2003): 3690–701. http://dx.doi.org/10.1128/jvi.77.6.3690-3701.2003.

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ABSTRACT Viruses utilize numerous mechanisms to counteract the host's immune response. Interferon production is a major component of the host antiviral response. Many viruses, therefore, produce proteins or RNA molecules that inhibit interferon-induced signal transduction pathways and their associated antiviral effects. Surprisingly, some viruses directly induce expression of interferon-induced genes. SM, an early lytic Epstein-Barr virus (EBV) nuclear protein, was found to specifically increase the expression of several genes (interferon-stimulated genes) that are known to be strongly induced by alpha/beta interferons. SM does not directly stimulate alpha/beta interferon secretion but instead induces STAT1, an intermediate step in the interferon signaling pathway. SM is a posttranscriptional activator of gene expression and increases STAT1 mRNA accumulation, particularly that of the functionally distinct STAT1β splice variant. SM expression in B lymphocytes is associated with decreased cell proliferation but does not decrease cell viability or induce cell cycle arrest. These results indicate that EBV can specifically induce cellular genes that are normally physiological targets of interferon by inducing components of cytokine signaling pathways. Our findings therefore suggest that some aspects of the interferon response may be positively modulated by infecting viruses.

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48

Winzer, Thilo, Valeria Gazda, Zhesi He, Filip Kaminski, Marcelo Kern, Tony R. Larson, Yi Li, et al. "A Papaver somniferum 10-Gene Cluster for Synthesis of the Anticancer Alkaloid Noscapine." Science 336, no. 6089 (May 31, 2012): 1704–8. http://dx.doi.org/10.1126/science.1220757.

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Noscapine is an antitumor alkaloid from opium poppy that binds tubulin, arrests metaphase, and induces apoptosis in dividing human cells. Elucidation of the biosynthetic pathway will enable improvement in the commercial production of noscapine and related bioactive molecules. Transcriptomic analysis revealed the exclusive expression of 10 genes encoding five distinct enzyme classes in a high noscapine–producing poppy variety, HN1. Analysis of an F2 mapping population indicated that these genes are tightly linked in HN1, and bacterial artificial chromosome sequencing confirmed that they exist as a complex gene cluster for plant alkaloids. Virus-induced gene silencing resulted in accumulation of pathway intermediates, allowing gene function to be linked to noscapine synthesis and a novel biosynthetic pathway to be proposed.

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49

Ye, Wenxiu, Eigo Ando, Mohammad Saidur Rhaman, Md Tahjib-Ul-Arif, Eiji Okuma, Yoshimasa Nakamura, Toshinori Kinoshita, and Yoshiyuki Murata. "Inhibition of light-induced stomatal opening by allyl isothiocyanate does not require guard cell cytosolic Ca2+ signaling." Journal of Experimental Botany 71, no. 10 (February 27, 2020): 2922–32. http://dx.doi.org/10.1093/jxb/eraa073.

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Abstract The glucosinolate–myrosinase system is a well-known defense system that has been shown to induce stomatal closure in Brassicales. Isothiocyanates are highly reactive hydrolysates of glucosinolates, and an isothiocyanate, allyl isothiocyanate (AITC), induces stomatal closure accompanied by elevation of free cytosolic Ca2+ concentration ([Ca2+]cyt) in Arabidopsis. It remains unknown whether AITC inhibits light-induced stomatal opening. This study investigated the role of Ca2+ in AITC-induced stomatal closure and inhibition of light-induced stomatal opening. AITC induced stomatal closure and inhibited light-induced stomatal opening in a dose-dependent manner. A Ca2+ channel inhibitor, La3+, a Ca2+chelator, EGTA, and an inhibitor of Ca2+ release from internal stores, nicotinamide, inhibited AITC-induced [Ca2+]cyt elevation and stomatal closure, but did not affect inhibition of light-induced stomatal opening. AITC activated non-selective Ca2+-permeable cation channels and inhibited inward-rectifying K+ (K+in) channels in a Ca2+-independent manner. AITC also inhibited stomatal opening induced by fusicoccin, a plasma membrane H+-ATPase activator, but had no significant effect on fusicoccin-induced phosphorylation of the penultimate threonine of H+-ATPase. Taken together, these results suggest that AITC induces Ca2+ influx and Ca2+ release to elevate [Ca2+]cyt, which is essential for AITC-induced stomatal closure but not for inhibition of K+in channels and light-induced stomatal opening.

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Lu, Min, David A. Lawrence, Scot Marsters, Diego Acosta-Alvear, Philipp Kimmig, Aaron S. Mendez, Adrienne W. Paton, James C. Paton, Peter Walter, and Avi Ashkenazi. "Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis." Science 345, no. 6192 (July 3, 2014): 98–101. http://dx.doi.org/10.1126/science.1254312.

Full text

Abstract:

Protein folding by the endoplasmic reticulum (ER) is physiologically critical; its disruption causes ER stress and augments disease. ER stress activates the unfolded protein response (UPR) to restore homeostasis. If stress persists, the UPR induces apoptotic cell death, but the mechanisms remain elusive. Here, we report that unmitigated ER stress promoted apoptosis through cell-autonomous, UPR-controlled activation of death receptor 5 (DR5). ER stressors induced DR5 transcription via the UPR mediator CHOP; however, the UPR sensor IRE1α transiently catalyzed DR5 mRNA decay, which allowed time for adaptation. Persistent ER stress built up intracellular DR5 protein, driving ligand-independent DR5 activation and apoptosis engagement via caspase-8. Thus, DR5 integrates opposing UPR signals to couple ER stress and apoptotic cell fate.

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Journal articles on the topic 'Science induces'

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