Structural Basis of PML-RARA Oncoprotein Targeting by Arsenic Unravels a Cysteine Rheostat Controlling PML Body Assembly and Function Article Swipe

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Pierre Bercier , Qian Qian Wang , Ning Zang , Jie Zhang , Chang Yang , Yasen Maimaitiyiming , Majdouline Abou-Ghali , Caroline Berthier , Chengchen Wu , Michiko Niwa‐Kawakita , Thassadite Dirami , Marie‐Claude Geoffroy , Omar Ferhi , Samuel Quentin , Shirine Benhenda , Yasumitsu Ogra , Zoher Gueroui , Chun Zhou , Hua Naranmandura , Hugues de Thé , Valérie Lallemand-Breitenbach ·

YOU? · · 2023 · Open Access · · DOI: https://doi.org/10.1158/2159-8290.cd-23-0453

PML nuclear bodies (NB) are disrupted in PML-RARA–driven acute promyelocytic leukemia (APL). Arsenic trioxide (ATO) cures 70% of patients with APL, driving PML-RARA degradation and NB reformation. In non-APL cells, arsenic binding onto PML also amplifies NB formation. Yet, the actual molecular mechanism(s) involved remain(s) elusive. Here, we establish that PML NBs display some features of liquid–liquid phase separation and that ATO induces a gel-like transition. PML B-box-2 structure reveals an alpha helix driving B2 trimerization and positioning a cysteine trio to form an ideal arsenic-binding pocket. Altering either of the latter impedes ATO-driven NB assembly, PML sumoylation, and PML-RARA degradation, mechanistically explaining clinical ATO resistance. This B2 trimer and the C213 trio create an oxidation-sensitive rheostat that controls PML NB assembly dynamics and downstream signaling in both basal state and during stress response. These findings identify the structural basis for arsenic targeting of PML that could pave the way to novel cancer drugs. Significance: Arsenic curative effects in APL rely on PML targeting. We report a PML B-box-2 structure that drives trimer assembly, positioning a cysteine trio to form an arsenic-binding pocket, which is disrupted in resistant patients. Identification of this ROS-sensitive triad controlling PML dynamics and functions could yield novel drugs. See related commentary by Salomoni, p. 2505. This article is featured in Selected Articles from This Issue, p. 2489

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Arsenic trioxide Trimer Chemistry Cysteine Function (biology) Arsenic Cell biology Cancer research Biochemistry Biology Dimer Enzyme Organic chemistry

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Type: article
Language: en
Landing Page: https://doi.org/10.1158/2159-8290.cd-23-0453
PDF: https://aacrjournals.org/cancerdiscovery/article-pdf/doi/10.1158/2159-8290.CD-23-0453/3361529/cd-23-0453.pdf
OA Status: hybrid
Cited By: 30
References: 84
Related Works: 10
OpenAlex ID: https://openalex.org/W4386346642

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OpenAlex ID: https://openalex.org/W4386346642

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DOI: https://doi.org/10.1158/2159-8290.cd-23-0453

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Title: Structural Basis of PML-RARA Oncoprotein Targeting by Arsenic Unravels a Cysteine Rheostat Controlling PML Body Assembly and Function

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Type: article

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Language: en

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Publication year: 2023

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Publication date: 2023-09-01

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Authors: Pierre Bercier, Qian Qian Wang, Ning Zang, Jie Zhang, Chang Yang, Yasen Maimaitiyiming, Majdouline Abou-Ghali, Caroline Berthier, Chengchen Wu, Michiko Niwa‐Kawakita, Thassadite Dirami, Marie‐Claude Geoffroy, Omar Ferhi, Samuel Quentin, Shirine Benhenda, Yasumitsu Ogra, Zoher Gueroui, Chun Zhou, Hua Naranmandura, Hugues de Thé, Valérie Lallemand-Breitenbach

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Landing page: https://doi.org/10.1158/2159-8290.cd-23-0453

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PDF URL: https://aacrjournals.org/cancerdiscovery/article-pdf/doi/10.1158/2159-8290.CD-23-0453/3361529/cd-23-0453.pdf

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Concepts: Arsenic trioxide, Trimer, Chemistry, Cysteine, Function (biology), Arsenic, Cell biology, Cancer research, Biochemistry, Biology, Dimer, Enzyme, Organic chemistry

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Cited by: 30

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Citations by year (recent): 2025: 14, 2024: 14, 2023: 2

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References (count): 84

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title	Structural Basis of PML-RARA Oncoprotein Targeting by Arsenic Unravels a Cysteine Rheostat Controlling PML Body Assembly and Function
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abstract_inverted_index.display	53
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abstract_inverted_index.pocket.	87
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abstract_inverted_index.reveals	70
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abstract_inverted_index.trioxide	14
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