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Journal articles on the topic 'Photoactivatable probe'

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Published: 9 March 2023

Last updated: 10 March 2023

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1

Kormos, Attila, Dóra Kern, Alexandra Egyed, Bianka Söveges, Krisztina Németh, and Péter Kele. "Microscope laser assisted photooxidative activation of bioorthogonal ClickOx probes." Chemical Communications 56, no. 40 (2020): 5425–28. http://dx.doi.org/10.1039/d0cc01512a.

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2

Tang, Juan, Mingshu Zhang, Hao-Yan Yin, Jing Jing, Da Xie, Pingyong Xu, and Jun-Long Zhang. "A photoactivatable Znsalen complex for super-resolution imaging of mitochondria in living cells." Chemical Communications 52, no. 77 (2016): 11583–86. http://dx.doi.org/10.1039/c6cc06531g.

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3

Peng, Qing, Yi Xia, Fanqi Qu, Xiaojun Wu, Daniel Campese, and Ling Peng. "Synthesis of a photoactivatable phospholipidic probe containing tetrafluorophenylazide." Tetrahedron Letters 46, no. 35 (August 2005): 5893–97. http://dx.doi.org/10.1016/j.tetlet.2005.06.125.

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4

Zhou, Xiaohong, Yuren Jiang, Xiongjie Zhao, and Dong Guo. "ESIPT-Based Photoactivatable Fluorescent Probe for Ratiometric Spatiotemporal Bioimaging." Sensors 16, no. 10 (October 12, 2016): 1684. http://dx.doi.org/10.3390/s16101684.

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5

Tirla, Alina, and Pablo Rivera-Fuentes. "Induction of Intracellular Reductive Stress with a Photoactivatable Phosphine Probe." CHIMIA International Journal for Chemistry 72, no. 4 (April 25, 2018): 241–44. http://dx.doi.org/10.2533/chimia.2018.241.

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6

Balas, Laurence, Malik Hellal, Jean-Claude Rossi, and Thierry Durand. "Synthesis of a photoactivatable probe of the anandamide re-uptake." Natural Product Research 19, no. 4 (June 2005): 419–23. http://dx.doi.org/10.1080/14786410500057015.

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7

SEYER, RENE, ANDRE AUMELAS, MARTINE TENCE, JACKY MARIE, JEAN-CLAUDE BONNAFOUS, SERGE JARD, and BERTRAND CASTRO. "Synthesis of a biotinylated, iodinatable, and photoactivatable probe for angiotensin receptors." International Journal of Peptide and Protein Research 34, no. 3 (January 12, 2009): 235–45. http://dx.doi.org/10.1111/j.1399-3011.1989.tb00236.x.

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8

Delfino, Jose M., Stuart L. Schreiber, and Frederic M. Richards. "Design, synthesis, and properties of a photoactivatable membrane-spanning phospholipidic probe." Journal of the American Chemical Society 115, no. 9 (May 1993): 3458–74. http://dx.doi.org/10.1021/ja00062a009.

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9

Verkhusha, Vladislav V., and Alexander Sorkin. "Conversion of the Monomeric Red Fluorescent Protein into a Photoactivatable Probe." Chemistry & Biology 12, no. 3 (March 2005): 279–85. http://dx.doi.org/10.1016/j.chembiol.2005.01.005.

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10

Welman, Arkadiusz, Alan Serrels, Valerie G. Brunton, Mark Ditzel, and Margaret C. Frame. "Two-color Photoactivatable Probe for Selective Tracking of Proteins and Cells." Journal of Biological Chemistry 285, no. 15 (February 5, 2010): 11607–16. http://dx.doi.org/10.1074/jbc.m110.102392.

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11

Wijesooriya, Chamari S., Julie A. Peterson, Pradeep Shrestha, Elizabeth J. Gehrmann, Arthur H. Winter, and Emily A. Smith. "A Photoactivatable BODIPY Probe for Localization-Based Super-Resolution Cellular Imaging." Angewandte Chemie 130, no. 39 (September 3, 2018): 12867–71. http://dx.doi.org/10.1002/ange.201805827.

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12

Wijesooriya, Chamari S., Julie A. Peterson, Pradeep Shrestha, Elizabeth J. Gehrmann, Arthur H. Winter, and Emily A. Smith. "A Photoactivatable BODIPY Probe for Localization-Based Super-Resolution Cellular Imaging." Angewandte Chemie International Edition 57, no. 39 (September 3, 2018): 12685–89. http://dx.doi.org/10.1002/anie.201805827.

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13

Lafreniere, Matthew A., Geneviève F. Desrochers, Kedous Mekbib, and John Paul Pezacki. "An affinity-based probe for methyltransferase enzymes based on sinefungin." Canadian Journal of Chemistry 95, no. 10 (October 2017): 1059–63. http://dx.doi.org/10.1139/cjc-2017-0168.

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Epigenetics control numerous cellular processes such as gene transcription, signal transduction, and protein stabilization. An understanding of epigenetic mechanisms can lead to the development of therapeutic agents for various diseases. Herein, we report the design and synthesis of a sinefungin affinity-probe (BpyneSF) that targets methyltranferase enzymes and proteins involved in recognition of methylation. This probe contains a bioorthogonal alkyne residue for conjugation using the copper-catalyzed azide–alkyne cycloaddition and a photoactivatable crosslinker group for covalent attachment of the probe to its proteomic targets. We investigate the efficiency and selectivity of the probe to inhibit and label methyltransferase enzymes, and we demonstrate, through in-gel fluorescence, on-bead digestion, and tandem mass spectrometry, that BpyneSF can label methyltransferase SETD2 and reader proteins in vitro. These results establish the utility of BpyneSF as a tool for affinity-based protein profiling in complex biological environments.

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14

Gu, Xiaodong, Ying Huang, Bruce S. Levison, Gary Gerstenecker, Anthony J. DiDonato, Leah B. Hazen, Joonsue Lee, Valentin Gogonea, Joseph A. DiDonato, and Stanley L. Hazen. "Identification of Critical Paraoxonase 1 Residues Involved in High Density Lipoprotein Interaction." Journal of Biological Chemistry 291, no. 4 (November 13, 2015): 1890–904. http://dx.doi.org/10.1074/jbc.m115.678334.

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Paraoxonase 1 (PON1) is a high density lipoprotein (HDL)-associated protein with atherosclerosis-protective and systemic anti-oxidant functions. We recently showed that PON1, myeloperoxidase, and HDL bind to one another in vivo forming a functional ternary complex (Huang, Y., Wu, Z., Riwanto, M., Gao, S., Levison, B. S., Gu, X., Fu, X., Wagner, M. A., Besler, C., Gerstenecker, G., Zhang, R., Li, X. M., Didonato, A. J., Gogonea, V., Tang, W. H., et al. (2013) J. Clin. Invest. 123, 3815–3828). However, specific residues on PON1 involved in the HDL-PON1 interaction remain unclear. Unambiguous identification of protein residues involved in docking interactions to lipid surfaces poses considerable methodological challenges. Here we describe a new strategy that uses a novel synthetic photoactivatable and click chemistry-taggable phospholipid probe, which, when incorporated into HDL, was used to identify amino acid residues on PON1 that directly interact with the lipoprotein phospholipid surface. Several specific PON1 residues (Leu-9, Tyr-185, and Tyr-293) were identified through covalent cross-links with the lipid probes using affinity isolation coupled to liquid chromatography with on-line tandem mass spectrometry. Based upon the crystal structure for PON1, the identified residues are all localized in relatively close proximity on the surface of PON1, defining a domain that binds to the HDL lipid surface. Site-specific mutagenesis of the identified PON1 residues (Leu-9, Tyr-185, and Tyr-293), coupled with functional studies, reveals their importance in PON1 binding to HDL and both PON1 catalytic activity and stability. Specifically, the residues identified on PON1 provide important structural insights into the PON1-HDL interaction. More generally, the new photoactivatable and affinity-tagged lipid probe developed herein should prove to be a valuable tool for identifying contact sites supporting protein interactions with lipid interfaces such as found on cell membranes or lipoproteins.

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15

Li, Jun, Yingcai Hu, Zuhao Li, Wei Liu, Ting Deng, and Jishan Li. "Photoactivatable Red Chemiluminescent AIEgen Probe for In Vitro/Vivo Imaging Assay of Hydrazine." Analytical Chemistry 93, no. 30 (July 23, 2021): 10601–10. http://dx.doi.org/10.1021/acs.analchem.1c01804.

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16

Halabi, Elias A., Zacharias Thiel, Nils Trapp, Dorothea Pinotsi, and Pablo Rivera-Fuentes. "A Photoactivatable Probe for Super-Resolution Imaging of Enzymatic Activity in Live Cells." Journal of the American Chemical Society 139, no. 37 (September 5, 2017): 13200–13207. http://dx.doi.org/10.1021/jacs.7b07748.

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17

Kilgour, Samantha L., Robert Jenkins, and Manuela Tosin. "A Photoactivatable Small‐Molecule Probe for the In Vivo Capture of Polyketide Intermediates." Chemistry – A European Journal 25, no. 72 (November 28, 2019): 16511–14. http://dx.doi.org/10.1002/chem.201903661.

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18

Chen, Lei, Yu Sun, Jinbo Li, and Yan Zhang. "A photoactivatable microRNA probe for identification of microRNA targets and light-controlled suppression of microRNA target expression." Chemical Communications 56, no. 4 (2020): 627–30. http://dx.doi.org/10.1039/c9cc08277h.

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19

Huang, Yepei, Xue Bai, Zhenchang Guo, Hanyang Dong, Yun Fu, Hui Zhang, Guijin Zhai, Shanshan Tian, Ye Wang, and Kai Zhang. "DNA-guided photoactivatable probe-based chemical proteomics reveals the reader protein of mRNA methylation." iScience 24, no. 9 (September 2021): 103046. http://dx.doi.org/10.1016/j.isci.2021.103046.

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20

Bell, Jessica L., Andrew J. Haak, Susan M. Wade, Yihan Sun, Richard R. Neubig, and Scott D. Larsen. "Design and synthesis of tag-free photoprobes for the identification of the molecular target for CCG-1423, a novel inhibitor of the Rho/MKL1/SRF signaling pathway." Beilstein Journal of Organic Chemistry 9 (May 21, 2013): 966–73. http://dx.doi.org/10.3762/bjoc.9.111.

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CCG-1423 and related analogues represent a new class of inhibitors of Rho/MKL1/SRF-mediated gene transcription, a pathway that has been implicated in both cancer and fibrosis. The molecular target for these compounds is unknown. To facilitate its identification, a series of tag-free photoaffinity probes was designed and synthesized, each one containing a photoactivatable group and an acetylenic end group for subsequent attachment to a fluorescent tag using click chemistry. All were confirmed to maintain biological activity in a cell-based assay for inhibition of SRE-Luc expression. The functional activity of the most potent probe 24 was further confirmed in an assay for PC-3 cell migration. Photolysis of 24 in intact PC-3 cells followed by cell lysis, click ligation of a fluorescent dye, and gel electrophoresis revealed specific labeling of a single 24 kDa band that could be blocked with an active competitor. Future work will focus on identifying the labeled protein(s).

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21

Radding, Jeffrey A., Steven A. Heidler, and William W. Turner. "Photoaffinity Analog of the Semisynthetic Echinocandin LY303366: Identification of Echinocandin Targets inCandida albicans." Antimicrobial Agents and Chemotherapy 42, no. 5 (May 1, 1998): 1187–94. http://dx.doi.org/10.1128/aac.42.5.1187.

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ABSTRACT The echinocandins are a family of cyclic lipopeptides with potent antifungal activity. These compounds inhibit the synthesis of β-1,3-glucan in fungi. The new semisynthetic echinocandin LY303366 was derivatized to produce a photoactivatable cross-linking echinocandin analog with antifungal activity. This analog was radioiodinated and used as a probe in microsomal membrane preparations of Candida albicans which contain glucan synthase activity. The photoaffinity probe identified two major proteins of 40 and 18 kDa in both membrane preparations. Labeling of these proteins was specific in that it required irradiation with UV light and was effectively competed against with unlabeled echinocandin analogs. In addition, the abilities of echinocandin analogs to compete with the photoaffinity probe correlated to their relative antifungal potencies and glucan synthase inhibition. The 40-kDa protein was isolated, and partial sequences were obtained from internal peptide fragments of the protein. Analysis of the sequences of these internal peptides of the 40-kDa protein revealed that it was a new protein not previously described as being involved in glucan synthesis or the mode of action of echinocandins.

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22

GUY, Mark R., Petr A. ILLARIONOV, Sudagar S. GURCHA, Lynn G. DOVER, Kevin J. C. GIBSON, Paul W. SMITH, David E. MINNIKIN, and Gurdyal S. BESRA. "Novel prenyl-linked benzophenone substrate analogues of mycobacterial mannosyltransferases." Biochemical Journal 382, no. 3 (September 7, 2004): 905–12. http://dx.doi.org/10.1042/bj20040911.

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PPM (polyprenol monophosphomannose) has been shown to act as a glycosyl donor in the biosynthesis of the Man (mannose)-rich mycobacterial lipoglycans LM (lipomannan) and LAM (lipoarabinomannan). The Mycobacterium tuberculosis PPM synthase (Mt-Ppm1) catalyses the transfer of Man from GDP-Man to polyprenyl phosphates. The resulting PPM then serves as a donor of Man residues leading to the formation of an α(1→6)LM intermediate through a PPM-dependent α(1→6)mannosyltransferase. In the present study, we prepared a series of ten novel prenyl-related photoactivatable probes based on benzophenone with lipophilic spacers replacing several internal isoprene units. These probes were excellent substrates for the recombinant PPM synthase Mt-Ppm1/D2 and, on photoactivation, several inhibited its activity in vitro. The protection of the PPM synthase activity by a ‘natural’ C75 polyprenyl acceptor during phototreatment is consistent with probe-mediated photoinhibition occurring via specific covalent modification of the enzyme active site. In addition, the unique mannosylated derivatives of the photoreactive probes were all donors of Man residues, through a PPM-dependent mycobacterial α(1→6)mannosyltransferase, to a synthetic Manp(1→6)-Manp-O-C10:1 disaccharide acceptor (where Manp stands for mannopyranose). Photoactivation of probe 7 led to striking-specific inhibition of the M. smegmatis α(1→6)mannosyltransferase. The present study represents the first application of photoreactive probes to the study of mycobacterial glycosyltransferases involved in LM and LAM biosynthesis. These preliminary findings suggest that the probes will prove useful in investigating the polyprenyl-dependent steps of the complex biosynthetic pathways to the mycobacterial lipoglycans, aiding in the identification of novel glycosyltransferases.

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23

Mangialavori, Irene C., Ana Maria Villamil Giraldo, Cristina Marino Buslje Marino Buslje, Mariela Ferreira Gomes, Ariel Caride, and Juan Pablo F. C. Rossi. "A New Conformation in SERCA and PMCA Ca2+ Pumps Revealed by a Photoactivatable Phospholipidic Probe." Biophysical Journal 96, no. 3 (February 2009): 614a. http://dx.doi.org/10.1016/j.bpj.2008.12.3246.

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24

Duval, Romain, Kevin Cottet, Magali Blaud, Anaïs Merckx, Sandrine Houzé, Philippe Grellier, Marie-Christine Lallemand, and Sylvie Michel. "A Photoalkylative Fluorogenic Probe of Guttiferone A for Live Cell Imaging and Proteome Labeling in Plasmodium falciparum." Molecules 25, no. 21 (November 4, 2020): 5139. http://dx.doi.org/10.3390/molecules25215139.

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Guttiferone A (GA) 1, a polycyclic polyprenylated acylphloroglucinol (PPAP) isolated from the plant Symphonia globulifera (Clusiaceae), constitutes a novel hit in antimalarial drug discovery. PPAPs do not possess identified biochemical targets in malarial parasites up to now. Towards this aim, we designed and evaluated a natural product-derived photoactivatable probe AZC-GA 5, embedding a photoalkylative fluorogenic motif of the 7-azidocoumarin (AZC) type, devoted to studying the affinity proteins interacting with GA in Plasmodium falciparum. Probe 5 manifested a number of positive functional and biological features, such as (i) inhibitory activity in vitro against P. falciparum blood-stages that was superimposable to that of GA 1, dose–response photoalkylative fluorogenic properties (ii) in model conditions using bovine serum albumin (BSA) as an affinity protein surrogate, (iii) in live P. falciparum-infected erythrocytes, and (iv) in fresh P. falciparum cell lysate. Fluorogenic signals by photoactivated AZC-GA 5 in biological settings were markedly abolished in the presence of excess GA 1 as a competitor, indicating significant pharmacological specificity of the designed molecular probe relative to the native PPAP. These results open the way to identify the detected plasmodial proteins as putative drug targets for the natural product 1 by means of proteomic analysis.

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25

Henry, Olivier, Fernando Lopez-Gallego, Sean A. Agger, Claudia Schmidt-Dannert, Stephanie Sen, David Shintani, Katrina Cornish, and Mark D. Distefano. "A versatile photoactivatable probe designed to label the diphosphate binding site of farnesyl diphosphate utilizing enzymes." Bioorganic & Medicinal Chemistry 17, no. 13 (July 2009): 4797–805. http://dx.doi.org/10.1016/j.bmc.2009.04.034.

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26

Mangialavori, Irene C., Mariela S. Ferreira Gomes, Maria F. Pignataro, Ana M. Villamil, Ariel J. Caride, Emanuel E. Strehler, and Juan Pablo F. Rossi. "Measuring the Dissociation Constants of Ligands from PMCA Complexes by a Photoactivatable Phosphatidylcholine Membrane Domain Probe." Biophysical Journal 98, no. 3 (January 2010): 169a. http://dx.doi.org/10.1016/j.bpj.2009.12.913.

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27

Alcaraz, Marie-Lyne, Ling Peng, Philippe Klotz, and Maurice Goeldner. "Synthesis and Properties of Photoactivatable Phospholipid Derivatives Designed To Probe the Membrane-Associate Domains of Proteins." Journal of Organic Chemistry 61, no. 1 (January 1996): 192–201. http://dx.doi.org/10.1021/jo951350k.

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28

Castello, P. R., A. J. Caride, F. L. G. Flecha, H. N. Fernandez, J. P. F. C. Rossi, and J. M. Delfino. "Identification of Transmembrane Domains of the Red Cell Calcium Pump with a New Photoactivatable Phospholipidic Probe." Biochemical and Biophysical Research Communications 201, no. 1 (May 1994): 194–200. http://dx.doi.org/10.1006/bbrc.1994.1688.

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29

Tirla, Alina, and Pablo Rivera-Fuentes. "Development of a Photoactivatable Phosphine Probe for Induction of Intracellular Reductive Stress with Single-Cell Precision." Angewandte Chemie International Edition 55, no. 47 (October 20, 2016): 14709–12. http://dx.doi.org/10.1002/anie.201608779.

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30

Tirla, Alina, and Pablo Rivera-Fuentes. "Development of a Photoactivatable Phosphine Probe for Induction of Intracellular Reductive Stress with Single-Cell Precision." Angewandte Chemie 128, no. 47 (October 20, 2016): 14929–32. http://dx.doi.org/10.1002/ange.201608779.

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31

Ambroise, Yves, Charles Mioskowski, Gérard Leblanc, and Bernard Rousseau. "Syntheses and properties of photoactivatable sugar derivatives designed to probe the sugar-binding site of melibiose permease." Bioorganic & Medicinal Chemistry Letters 10, no. 10 (May 2000): 1125–27. http://dx.doi.org/10.1016/s0960-894x(00)00180-3.

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32

Izeddin, Ignacio, Christian G. Specht, Mickaël Lelek, Christophe Zimmer, Antoine Triller, Xavier Darzacq, and Maxime Dahan. "Long-Term Super-Resolution Imaging of Actin Cytoeskeleton in Dendritic Spines Using a Low-Affinity Photoactivatable Probe." Biophysical Journal 98, no. 3 (January 2010): 396a. http://dx.doi.org/10.1016/j.bpj.2009.12.2134.

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33

Bernardi, Dan, Eric Battaglia, and Gilbert Kirsch. "Synthesis and evaluation of an N-acylated photoactivatable analogue of glutathione as probe for glutathione-utilizing enzymes." Bioorganic & Medicinal Chemistry Letters 16, no. 6 (March 2006): 1601–4. http://dx.doi.org/10.1016/j.bmcl.2005.12.047.

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34

Wang, Xiao-Ming, Ruddy Wattiez, Fabien Brossier, Michele Mock, Paul Falmagne, Jean-Marie Ruysschaert, and Veronique Cabiaux. "Use of a photoactivatable lipid to probe the topology of PA63 of Bacillus anthracis in lipid membranes." European Journal of Biochemistry 256, no. 1 (August 15, 1998): 179–83. http://dx.doi.org/10.1046/j.1432-1327.1998.2560179.x.

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35

Fernandez, Asia M., Gregorio Fernandez-Ballester, Jose A. Ferragut, and Jose M. Gonzales-Ros. "Labeling of the nicotinic acetylcholine receptor by a photoactivatable steroid probe: effects of cholesterol and cholinergic ligands." Biochimica et Biophysica Acta (BBA) - Biomembranes 1149, no. 1 (June 1993): 135–44. http://dx.doi.org/10.1016/0005-2736(93)90034-w.

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36

Stewart-Ornstein, Jacob, Susan Chen, Rajat Bhatnagar, Jonathan S. Weissman, and Hana El-Samad. "Model-guided optogenetic study of PKA signaling in budding yeast." Molecular Biology of the Cell 28, no. 1 (January 2017): 221–27. http://dx.doi.org/10.1091/mbc.e16-06-0354.

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In eukaryotes, protein kinase A (PKA) is a master regulator of cell proliferation and survival. The activity of PKA is subject to elaborate control and exhibits complex time dynamics. To probe the quantitative attributes of PKA dynamics in the yeast Saccharomyces cerevisiae, we developed an optogenetic strategy that uses a photoactivatable adenylate cyclase to achieve real-time regulation of cAMP and the PKA pathway. We capitalize on the precise and rapid control afforded by this optogenetic tool, together with quantitative computational modeling, to study the properties of feedback in the PKA signaling network and dissect the nonintuitive dynamic effects that ensue from perturbing its components. Our analyses reveal that negative feedback channeled through the Ras1/2 GTPase is delayed, pinpointing its time scale and its contribution to the dynamic features of the cAMP/PKA signaling network.

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37

Kaur, Navpreet, Pranav Tiwari, Nirmiti Mate, Vinay Sharma, and Shaikh M. Mobin. "Photoactivatable carbon dots as a label-free fluorescent probe for picric acid detection and light-induced bacterial inactivation." Journal of Photochemistry and Photobiology B: Biology 229 (April 2022): 112412. http://dx.doi.org/10.1016/j.jphotobiol.2022.112412.

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38

Ross, W., W. Bertrand, and A. Morrison. "A photoactivatable probe for the Na+/H+ exchanger cross-links a 66-kDa renal brush border membrane protein." Journal of Biological Chemistry 265, no. 10 (April 1990): 5341–44. http://dx.doi.org/10.1016/s0021-9258(19)39360-3.

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39

Rossi, Juan P. F. C., Jose M. Delfino, Ariel J. Caride, and Horacio N. Fernandez. "Interaction of Unsaturated Fatty Acids with the Red Blood Cell Ca2+-ATPase. Studies with a Novel Photoactivatable Probe." Biochemistry 34, no. 11 (March 21, 1995): 3802–12. http://dx.doi.org/10.1021/bi00011a038.

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40

ALCARAZ, M. L., L. PENG, P. KLOTZ, and M. GOELDNER. "ChemInform Abstract: Synthesis and Properties of Photoactivatable Phospholipid Derivatives Designed to Probe the Membrane-Associate Domains of Proteins." ChemInform 27, no. 20 (August 5, 2010): no. http://dx.doi.org/10.1002/chin.199620207.

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41

Daneshjou, Nazila, Nathan Sieracki, Geerten P. van Nieuw Amerongen, Daniel E. Conway, Martin A. Schwartz, Yulia A. Komarova, and Asrar B. Malik. "Rac1 functions as a reversible tension modulator to stabilize VE-cadherin trans-interaction." Journal of Cell Biology 208, no. 1 (January 5, 2015): 23–32. http://dx.doi.org/10.1083/jcb.201409108.

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The role of the RhoGTPase Rac1 in stabilizing mature endothelial adherens junctions (AJs) is not well understood. In this paper, using a photoactivatable probe to control Rac1 activity at AJs, we addressed the relationship between Rac1 and the dynamics of vascular endothelial cadherin (VE-cadherin). We demonstrated that Rac1 activation reduced the rate of VE-cadherin dissociation, leading to increased density of VE-cadherin at AJs. This response was coupled to a reduction in actomyosin-dependent tension across VE-cadherin adhesion sites. We observed that inhibiting myosin II directly or through photo-release of the caged Rho kinase inhibitor also reduced the rate of VE-cadherin dissociation. Thus, Rac1 functions by stabilizing VE-cadherin trans-dimers in mature AJs by counteracting the actomyosin tension. The results suggest a new model of VE-cadherin adhesive interaction mediated by Rac1-induced reduction of mechanical tension at AJs, resulting in the stabilization of VE-cadherin adhesions.

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42

Mangialavori, Irene, Ana María Villamil Giraldo, Cristina Marino Buslje, Mariela Ferreira Gomes, Ariel J. Caride, and Juan Pablo F. C. Rossi. "A New Conformation in Sarcoplasmic Reticulum Calcium Pump and Plasma Membrane Ca2+Pumps Revealed by a Photoactivatable Phospholipidic Probe." Journal of Biological Chemistry 284, no. 8 (December 12, 2008): 4823–28. http://dx.doi.org/10.1074/jbc.m806912200.

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43

MODHA, J., M. C. ROBERTS, M. W. KENNEDY, and J. R. KUSEL. "Induction of surface fluidity in Trichinella spiralis larvae during penetration of the host intestine: simulation by cyclic AMP in vitro." Parasitology 114, no. 1 (January 1997): 71–77. http://dx.doi.org/10.1017/s0031182096008025.

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The lateral diffusion (DL) properties of the fluorescent lipid probe 5-N (octadecanoyl) aminofluorescein (AF18) inserted into the surface of muscle-stage larvae of Trichinella spiralis were investigated by fluorescence recovery after photobleaching. AF18 was not free to diffuse laterally in dormant larvae, and this remained unchanged after larval activation in vitro with trypsin and bile. However, a significant increase in surface fluidity of the probe was demonstrated (%R = 74·5; DL = 11·5 × 10−9 cm2/sec) when larvae invaded intestinal epithelial tissue following oral infection of mice. Membrane-permeant photoactivatable caged cyclic AMP was used to analyse the putative mechanism responsible for this increase in lateral diffusion in the parasite surface. Although incubation of larvae with 1–50 μM caged cAMP had no effect on surface fluidity, incubation with 100 μM caged cAMP induced a substantial increase in the lateral mobility of AF18 (%R = 64·3; DL = 8·3 × 10−11 cm2/sec) immediately following photo-activation of the caged messenger. This induced fluidity, however, was transient and the larval surface reverted to immobility within 15 min. These observations constitute the first reported measurement of the fluid properties of the surface of intracellular parasites, the first demonstration of the parasite surface fluidity altering as a result of host cell invasion and the first indication of a mechanism underlying changes in surface fluidity in parasitic helminths.

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44

Spillier, Quentin, Séverine Ravez, Simon Dochain, Didier Vertommen, Léopold Thabault, Olivier Feron, and Raphaël Frédérick. "Unravelling the Allosteric Targeting of PHGDH at the ACT-Binding Domain with a Photoactivatable Diazirine Probe and Mass Spectrometry Experiments." Molecules 26, no. 2 (January 18, 2021): 477. http://dx.doi.org/10.3390/molecules26020477.

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The serine biosynthetic pathway is a key element contributing to tumor proliferation. In recent years, targeting of phosphoglycerate dehydrogenase (PHGDH), the first enzyme of this pathway, intensified and revealed to be a promising strategy to develop new anticancer drugs. Among attractive PHGDH inhibitors are the α-ketothioamides. In previous work, we have demonstrated their efficacy in the inhibition of PHGDH in vitro and in cellulo. However, the precise site of action of this series, which would help the rational design of new inhibitors, remained undefined. In the present study, the detailed mechanism-of-action of a representative α-ketothioamide inhibitor is reported using several complementary experimental techniques. Strikingly, our work led to the identification of an allosteric site on PHGDH that can be targeted for drug development. Using mass spectrometry experiments and an original α-ketothioamide diazirine-based photoaffinity probe, we identified the 523Q-533F sequence on the ACT regulatory domain of PHGDH as the binding site of α-ketothioamides. Mutagenesis experiments further documented the specificity of our compound at this allosteric site. Our results thus pave the way for the development of new anticancer drugs using a completely novel mechanism-of-action.

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Wadzinski, B. E., M. F. Shanahan, R. B. Clark, and A. E. Ruoho. "Identification of the glucose transporter in mammalian cell membranes with a125I-forskolin photoaffinity label." Biochemical Journal 255, no. 3 (November 1, 1988): 983–90. http://dx.doi.org/10.1042/bj2550983.

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The glucose transporter has been identified in a variety of mammalian cell membranes using a photoactivatable carrier-free radioiodinated derivative of forskolin, 3-[125I]iodo-4-azidophenethylamido-7-O-succinyldeacetylforskoli n ([125I]IAPS-forskolin) at 1-3 nM. The membranes that were photolabelled with [125I]IAPS-forskolin were human placental membranes, rat cortical and cerebellar synaptic membranes, rat cardiac sarcolemmal membranes, rat adipocyte plasma membranes, smooth-muscle membranes, and S49 wild-type (WT) lymphoma-cell membranes. The glucose transporter in plasma membranes prepared from the insulin-responsive rat cardiac sarcolemmal cells, rat adipocytes and smooth-muscle cells were determined to be approx. 45 kDa by SDS/polyacrylamide-gel electrophoresis (PAGE). Photolysis of human placental membranes, rat cortical and cerebellar synaptic membranes, and WT lymphoma membranes with [125I]-IAPS-forskolin, followed by SDS/PAGE, indicated specific derivatization of a broad band (43-55 kDa) in placental membranes and a narrower band (approx. 45 kDa) in synaptic membranes and WT lymphoma membranes. Digestion of the [125I]IAPS-forskolin-labelled placental and WT lymphoma membranes with endo-beta-galactosidase showed a reduction in the apparent molecular mass of the radiolabelled band to approx. 40 kDa. The membranes that were photolabelled with [125I]IAPS-forskolin and trypsin-treated produced a radiolabelled proteolytic fragment with an apparent molecular mass of 18 kDa. [125I]IAPS-forskolin is a highly effective probe for identifying low levels of glucose transporters in mammalian tissues.

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Chu, Haiyan, Joseph F. Hoffman, and Philip S. Low. "Preliminary Identification of ATP Compartment Associated Proteins On Erythrocyte Membrane." Blood 114, no. 22 (November 20, 2009): 3019. http://dx.doi.org/10.1182/blood.v114.22.3019.3019.

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Abstract Abstract 3019 Poster Board II-995 A compartment/pool of ATP that is generated by glycolytic enzymes has been reported to exist on the erythrocyte membrane where it channels ATP directly to the Na+/K+-ATPase (Proverbio F and Hoffman JF. J. Gen. Physiol. 1977, 69:605-632. Mercer RW and Dunham PB. J. Gen. Physiol. 1981, 78:547-567). In order to identify the protein components enclosing this compartment of ATP, a photoactivatable probe, 8-azido-[αa-32P]ATP, was loaded into porous erythrocytes under conditions that fill the compartment with ATP, and the radiolabeled ATP was induced to label proximal proteins by illumination with UV light. Analysis of radiolabeled bands reveals that spectrin, adducin, protein 4.1, and actin constitute major components of the compartment. To further verify the involvement of these proteins in the ATP compartment, antibodies against the aforementioned proteins were pre-incubated with porous erythrocytes before attempting to load the compartment with ATP. Analysis of the efficiency of ATP loading in the presence of these blocking antibodies reveals that antibody binding prevents normal filling of the ATP pool. These findings confirm Hoffman's earlier hypothesis that a membrane-bound compartment of ATP exists. The data also suggest that the location of the compartment might reside at the junctional complex, and that the complex of enzymes that fill the ATP pool is different from the complex organized around band 3. Disclosures No relevant conflicts of interest to declare.

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Hyland, Caroline, Laurent Vuillard, Colin Hughes, and Vassilis Koronakis. "Membrane Interaction of Escherichia coliHemolysin: Flotation and Insertion-Dependent Labeling by Phospholipid Vesicles." Journal of Bacteriology 183, no. 18 (September 15, 2001): 5364–70. http://dx.doi.org/10.1128/jb.183.18.5364-5370.2001.

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ABSTRACT The 1,024-amino-acid acylated hemolysin of Escherichia coli subverts host cell functions and causes cell lysis. Both activities require insertion of the toxin into target mammalian cell membranes. To identify directly the principal toxin sequences dictating membrane binding and insertion, we assayed the lipid bilayer interaction of native protoxin, stably active toxin, and recombinant peptides. Binding was assessed by flotation of protein-liposome mixtures through density gradients, and insertion was assessed by labeling with a photoactivatable probe incorporated into the target lipid bilayer. Both the active acylated hemolysin and the inactive unacylated protoxin were able to bind and also insert. Ca2+binding, which is required for toxin activity, did not influence the in vitro interaction with liposomes. Three overlapping large peptides were expressed separately. A C-terminal peptide including residues 601 to 1024 did not interact in either assay. An internal peptide spanning residues 496 to 831, including the two acylation sites, bound to phospholipid vesicles and showed a low level of insertion-dependent labeling. In vitro acylation had no effect on the bilayer interaction of either this peptide or the full-length protoxin. An N-terminal peptide comprising residues 1 to 520 also bound to phospholipid vesicles and showed strong insertion-dependent labeling, ca. 5- to 25-fold that of the internal peptide. Generation of five smaller peptides from the N-terminal region identified the principal determinant of lipid insertion as the hydrophobic sequence encompassing residues 177 to 411, which is conserved among hemolysin-related toxins.

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Raviv, Yossef, Robert Blumenthal, S. Mark Tompkins, Jennifer Humberd, Robert J. Hogan, and Mathias Viard. "Hydrophobic Inactivation of Influenza Viruses Confers Preservation of Viral Structure with Enhanced Immunogenicity." Journal of Virology 82, no. 9 (February 27, 2008): 4612–19. http://dx.doi.org/10.1128/jvi.02233-07.

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ABSTRACT The use of inactivated influenza virus for the development of vaccines with broad heterosubtypic protection requires selective inactivation techniques that eliminate viral infectivity while preserving structural integrity. Here we tested if a hydrophobic inactivation approach reported for retroviruses could be applied to the influenza virus. By this approach, the transmembrane domains of viral envelope proteins are selectively targeted by the hydrophobic photoactivatable compound 1,5-iodonaphthyl-azide (INA). This probe partitions into the lipid bilayer of the viral envelope and upon far UV irradiation reacts selectively with membrane-embedded domains of proteins and lipids while the protein domains that localize outside the bilayer remain unaffected. INA treatment of influenza virus blocked infection in a dose-dependent manner without disrupting the virion or affecting neuraminidase activity. Moreover, the virus maintained the full activity in inducing pH-dependent lipid mixing, but pH-dependent redistribution of viral envelope proteins into the target cell membrane was completely blocked. These results indicate that INA selectively blocks fusion of the virus with the target cell membrane at the pore formation and expansion step. Using a murine model of influenza virus infection, INA-inactivated influenza virus induced potent anti-influenza virus serum antibody and T-cell responses, similar to live virus immunization, and protected against heterosubtypic challenge. INA treatment of influenza A virus produced a virus that is noninfectious, intact, and fully maintains the functional activity associated with the ectodomains of its two major envelope proteins, neuraminidase and hemagglutinin. When used as a vaccine given intranasally (i.n.), INA-inactivated influenza virus induced immune responses similar to live virus infection.

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Vaillancourt, R. R., N. Dhanasekaran, and A. E. Ruoho. "The photoactivatable NAD+ analogue [32P]2-azido-NAD+ defines intra- and inter-molecular interactions of the C-terminal domain of the G-protein Gαt." Biochemical Journal 311, no. 3 (November 1, 1995): 987–93. http://dx.doi.org/10.1042/bj3110987.

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Recently, we reported the synthesis and use of [32P]2-azido-NAD+ as a probe to study the structural organization of G-proteins. Pertussis toxin was used to ‘tether’ [32P]2-azido-ADP-ribose of [32P]2-azido-NAD+ to Cys347 of the alpha subunit of the G-protein Gt. Light activation of the azide moiety covalently cross-linked the domain containing Cys347 at the C-terminus of alpha t with neighbouring intra- and inter-molecular domains of holo-transducin. The radiolabel from [32P]2-azido-ADP-ribose was then transferred to the ‘acceptor’ domain by cleaving the thioglycosidic bond between Cys347 and [32P]2-azido-ADP- ribose with mercuric acetate. ADP-ribosylation followed by photocross-linking of holo-transducin indicated intramolecular interactions of the C-terminal domain with other alpha t domains and intermolecular interactions with holotransducin alpha and gamma subunits. The radiolabelled peptides, which were radiolabelled because of the transfer of the photoactive moiety, were identified by utilizing 2-(2′-nitrophenylsulphenyl)-3-methyl-3′- bromoindolenine (‘BNPS-skatole’) and CNBr. The results indicate that the C-terminus of alpha t interacts with both N-terminal and C-terminal domains within the alpha t molecular. Mapping the interacting sites between cross-linked alpha dimers and alpha trimers indicates that the C-terminal domain of alpha t is involved in the formation of alpha t homopolymers in solution. In addition, our studies place the beta gamma subunit in close proximity to Cys347 of alpha t, as indicated by the transfer of [32P]2-azido-ADP-ribose from Cys347 to the gamma subunit, which was further localized to the C-terminal half of gamma t. The studies presented here identify the C-terminal intra- and inter-molecular interactions of the alpha subunit of holo-transducin.

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Zettl, R., J. Feldwisch, W. Boland, J. Schell, and K. Palme. "5'-Azido-[3,6-3H2]-1-napthylphthalamic acid, a photoactivatable probe for naphthylphthalamic acid receptor proteins from higher plants: identification of a 23-kDa protein from maize coleoptile plasma membranes." Proceedings of the National Academy of Sciences 89, no. 2 (January 15, 1992): 480–84. http://dx.doi.org/10.1073/pnas.89.2.480.

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