ID | 65505 |
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Author |
Matsumoto, Yoshinori
Department of Nephrology, Rheumatology, Endocrinology and Metabolism, Okayama University Faculty of Medicine, Dentistry and Pharmaceutical Sciences
Kaken ID
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Rottapel, Robert
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Abstract | Modification of proteins by ADP-ribose (PARsylation) is catalyzed by the poly(ADP-ribose) polymerase (PARP) family of enzymes exemplified by PARP1, which controls chromatin organization and DNA repair. Additionally, PARsylation induces ubiquitylation and proteasomal degradation of its substrates because PARsylation creates a recognition site for E3-ubiquitin ligase. The steady-state levels of the adaptor protein SH3-domain binding protein 2 (3BP2) is negatively regulated by tankyrase (PARP5), which coordinates ubiquitylation of 3BP2 by the E3-ligase ring finger protein 146 (RNF146). 3BP2 missense mutations uncouple 3BP2 from tankyrase-mediated negative regulation and cause Cherubism, an autosomal dominant autoinflammatory disorder associated with craniofacial dysmorphia. In this review, we summarize the diverse biological processes, including bone dynamics, metabolism, and Toll-like receptor (TLR) signaling controlled by tankyrase-mediated PARsylation of 3BP2, and highlight the therapeutic potential of this pathway.
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Keywords | PARsylation
ubiquitylation
proteasomal degradation
Cherubism
tankyrase
PARPs
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Published Date | 2023-05
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Publication Title |
Trends in Molecular Medicine
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Volume | volume29
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Issue | issue5
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Publisher | Elsevier BV
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Start Page | 390
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End Page | 405
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ISSN | 1471-4914
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Content Type |
Journal Article
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language |
English
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OAI-PMH Set |
岡山大学
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Copyright Holders | © 2023 The Authors.
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File Version | publisher
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Related Url | isVersionOf https://doi.org/10.1016/j.molmed.2023.02.001
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License | http://creativecommons.org/licenses/by/4.0/
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