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9. Poly ADP-ribose signaling is dysregulated in Huntington disease.

Author

Tamara Maiuri, Barba Bazan, Carlos, Harding, Rachel J., Begeja, Nola, Tae-In Kam, Byrne, Lauren M., Rodrigues, Filipe B., Warner, Monica M., Neuman, Kaitlyn, Mansoor, Muqtasid, Badiee, Mohsen, Dasovich, Morgan, Keona Wang, Thompson, Leslie M., Leung, Anthony K. L., Andres, Sara N., Wild, Edward J., Dawson, Ted M., Dawson, Valina L., and Arrowsmith, Cheryl H.

Subjects
HUNTINGTON disease, SINGLE molecules, GENOME-wide association studies, ATOMIC force microscopy, DNA repair
Abstract

Huntington disease (HD) is a genetic neurodegenerative disease caused by cytosine, adenine, guanine (CAG) expansion in the Huntingtin (HTT) gene, translating to an expanded polyglutamine tract in the HTT protein. Age at disease onset correlates to CAG repeat length but varies by decades between individuals with identical repeat lengths. Genome-wide association studies link HD modification to DNA repair and mitochondrial health pathways. Clinical studies show elevated DNA damage in HD, even at the premanifest stage. A major DNA repair node influencing neurodegenerative disease is the PARP pathway. Accumulation of poly adenosine diphosphate (ADP)-ribose (PAR) has been implicated in Alzheimer and Parkinson diseases, as well as cerebellar ataxia. We report that HD mutation carriers have lower cerebrospinal fluid PAR levels than healthy controls, starting at the premanifest stage. Human HD induced pluripotent stem cell-derived neurons and patient-derived fibroblasts have diminished PAR response in the context of elevated DNA damage. We have defined a PAR-binding motif in HTT, detected HTT complexed with PARylated proteins in human cells during stress, and localized HTT to mitotic chromosomes upon inhibition of PAR degradation. Direct HTT PAR binding was measured by fluorescence polarization and visualized by atomic force microscopy at the single molecule level. While wild-type and mutant HTT did not differ in their PAR binding ability, purified wild-type HTT protein increased in vitro PARP1 activity while mutant HTT did not. These results provide insight into an early molecular mechanism of HD, suggesting possible targets for the design of early preventive therapies. [ABSTRACT FROM AUTHOR]

Published
2024
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24. Poly ADP-Ribose Signaling is Dysregulated in Huntington’s Disease Patients

Author

Maiuri, Tamara, primary, Bazan, Carlos Barba, additional, Harding, Rachel J., additional, Begeja, Nola, additional, Kam, Tae-In, additional, Byrne, Lauren M., additional, Rodrigues, Filipe B., additional, Warner, Monica M., additional, Neuman, Kaitlyn, additional, Mansoor, Muqtasid, additional, Badiee, Mohsen, additional, Dasovich, Morgan, additional, Leung, Anthony K. L., additional, Andres, Sara N., additional, Wild, Edward J., additional, Dawson, Ted M., additional, Dawson, Valina L., additional, Arrowsmith, Cheryl H., additional, and Truant, Ray, additional

Published
2022
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25. Poly(ADP-ribose) promotes toxicity of C9ORF72 arginine-rich dipeptide repeat proteins

Author

Gao, Junli, primary, Mewborne, Quinlan T., additional, Girdhar, Amandeep, additional, Sheth, Udit, additional, Coyne, Alyssa N., additional, Punathil, Ritika, additional, Kang, Bong Gu, additional, Dasovich, Morgan, additional, Veire, Austin, additional, DeJesus Hernandez, Mariely, additional, Liu, Shuaichen, additional, Shi, Zheng, additional, Dafinca, Ruxandra, additional, Fouquerel, Elise, additional, Talbot, Kevin, additional, Kam, Tae-In, additional, Zhang, Yong-Jie, additional, Dickson, Dennis, additional, Petrucelli, Leonard, additional, van Blitterswijk, Marka, additional, Guo, Lin, additional, Dawson, Ted M., additional, Dawson, Valina L., additional, Leung, Anthony K. L., additional, Lloyd, Thomas E., additional, Gendron, Tania F., additional, Rothstein, Jeffrey D., additional, and Zhang, Ke, additional

Published
2022
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28. ADP-ribosyltransferases, an update on function and nomenclature

Author

Lüscher, Bernhard, Ahel, Ivan, Altmeyer, Matthias, Ashworth, Alan, Bai, Peter, Chang, Paul, Cohen, Michael, Corda, Daniela, Dantzer, Francoise, Daugherty, Matthew D., Dawson, Ted M., Dawson, Valina L., Deindl, Sebastian, Fehr, Anthony R., Feijs, Karla L. H., Filippov, Dmitri V., Gagné, Jean-Philippe, Grimaldi, Giovanna, Guettler, Sebastian, Hoch, Nicolas C., Hottiger, Michael O., Korn, Patricia, Kraus, W. Lee, Ladurner, Andreas, Lehtiö, Lari, Leung, Anthony K. L., Lord, Christopher J., Mangerich, Aswin, Matic, Ivan, Matthews, Jason, Moldovan, George-Lucian, Moss, Joel, Natoli, Gioacchino, Nielsen, Michael L., Niepel, Mario, Nolte, Friedrich, Pascal, John, Paschal, Bryce M., Pawlowski, Krzysztof, Poirier, Guy G., Smith, Susan, Timinszky, Gyula, Wang, Zhao-Qi, Yelamos, Jose, Yu, Xiaochun, Zaja, Roko, Ziegler, Mathias, Lüscher, Bernhard, Ahel, Ivan, Altmeyer, Matthias, Ashworth, Alan, Bai, Peter, Chang, Paul, Cohen, Michael, Corda, Daniela, Dantzer, Francoise, Daugherty, Matthew D., Dawson, Ted M., Dawson, Valina L., Deindl, Sebastian, Fehr, Anthony R., Feijs, Karla L. H., Filippov, Dmitri V., Gagné, Jean-Philippe, Grimaldi, Giovanna, Guettler, Sebastian, Hoch, Nicolas C., Hottiger, Michael O., Korn, Patricia, Kraus, W. Lee, Ladurner, Andreas, Lehtiö, Lari, Leung, Anthony K. L., Lord, Christopher J., Mangerich, Aswin, Matic, Ivan, Matthews, Jason, Moldovan, George-Lucian, Moss, Joel, Natoli, Gioacchino, Nielsen, Michael L., Niepel, Mario, Nolte, Friedrich, Pascal, John, Paschal, Bryce M., Pawlowski, Krzysztof, Poirier, Guy G., Smith, Susan, Timinszky, Gyula, Wang, Zhao-Qi, Yelamos, Jose, Yu, Xiaochun, Zaja, Roko, and Ziegler, Mathias

Abstract

ADP-ribosylation, a modification of proteins, nucleic acids, and metabolites, confers broad functions, including roles in stress responses elicited, for example, by DNA damage and viral infection and is involved in intra- and extracellular signaling, chromatin and transcriptional regulation, protein biosynthesis, and cell death. ADP-ribosylation is catalyzed by ADP-ribosyltransferases (ARTs), which transfer ADP-ribose from NAD+ onto substrates. The modification, which occurs as mono- or poly-ADP-ribosylation, is reversible due to the action of different ADP-ribosylhydrolases. Importantly, inhibitors of ARTs are approved or are being developed for clinical use. Moreover, ADP-ribosylhydrolases are being assessed as therapeutic targets, foremost as antiviral drugs and for oncological indications. Due to the development of novel reagents and major technological advances that allow the study of ADP-ribosylation in unprecedented detail, an increasing number of cellular processes and pathways are being identified that are regulated by ADP-ribosylation. In addition, characterization of biochemical and structural aspects of the ARTs and their catalytic activities have expanded our understanding of this protein family. This increased knowledge requires that a common nomenclature be used to describe the relevant enzymes. Therefore, in this viewpoint, we propose an updated and broadly supported nomenclature for mammalian ARTs that will facilitate future discussions when addressing the biochemistry and biology of ADP-ribosylation. This is combined with a brief description of the main functions of mammalian ARTs to illustrate the increasing diversity of mono- and poly-ADP-ribose mediated cellular processes.

Published
2022
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31. High-Throughput Activity Assay for Screening Inhibitors of the SARS-CoV-2 Mac1 Macrodomain

Author

Dasovich, Morgan, primary, Zhuo, Junlin, additional, Goodman, Jack A., additional, Thomas, Ajit, additional, McPherson, Robert Lyle, additional, Jayabalan, Aravinth Kumar, additional, Busa, Veronica F., additional, Cheng, Shang-Jung, additional, Murphy, Brennan A., additional, Redinger, Karli R., additional, Alhammad, Yousef M. O., additional, Fehr, Anthony R., additional, Tsukamoto, Takashi, additional, Slusher, Barbara S., additional, Bosch, Jürgen, additional, Wei, Huijun, additional, and Leung, Anthony K. L., additional

Published
2021
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35. ADP‐ribosyltransferases, an update on function and nomenclature

Author

Lüscher, Bernhard, primary, Ahel, Ivan, additional, Altmeyer, Matthias, additional, Ashworth, Alan, additional, Bai, Peter, additional, Chang, Paul, additional, Cohen, Michael, additional, Corda, Daniela, additional, Dantzer, Françoise, additional, Daugherty, Matthew D., additional, Dawson, Ted M., additional, Dawson, Valina L., additional, Deindl, Sebastian, additional, Fehr, Anthony R., additional, Feijs, Karla L. H., additional, Filippov, Dmitri V., additional, Gagné, Jean‐Philippe, additional, Grimaldi, Giovanna, additional, Guettler, Sebastian, additional, Hoch, Nicolas C., additional, Hottiger, Michael O., additional, Korn, Patricia, additional, Kraus, W. Lee, additional, Ladurner, Andreas, additional, Lehtiö, Lari, additional, Leung, Anthony K. L., additional, Lord, Christopher J., additional, Mangerich, Aswin, additional, Matic, Ivan, additional, Matthews, Jason, additional, Moldovan, George‐Lucian, additional, Moss, Joel, additional, Natoli, Gioacchino, additional, Nielsen, Michael L., additional, Niepel, Mario, additional, Nolte, Friedrich, additional, Pascal, John, additional, Paschal, Bryce M., additional, Pawłowski, Krzysztof, additional, Poirier, Guy G., additional, Smith, Susan, additional, Timinszky, Gyula, additional, Wang, Zhao‐Qi, additional, Yélamos, José, additional, Yu, Xiaochun, additional, Zaja, Roko, additional, and Ziegler, Mathias, additional

Published
2021
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39. Nucleolar proteome dynamics

Author

Andersen, Jens S., Lam, Yun W., Leung, Anthony K. L., Ong, Shao-En, Lyon, Carol E., Lamond, Angus I., and Mann, Matthias

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Jens S. Andersen [1, 4]; Yun W. Lam [2, 4]; Anthony K. L. Leung [2, 3]; Shao-En Ong [1]; Carol E. Lyon [2]; Angus I. Lamond (corresponding author) [2]; [...]

Published
2005
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