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

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

doi:10.1158/2159-8290.cd-23-0453

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

Pierre Bercier , Shirine Benhenda + Show 19 more

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

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Journal: Cancer Discovery	Publication Date: Sep 1, 2023
Citations: 8	License type: CC BY-NC-ND 4.0

Affiliation: Université Paris Sciences et Lettres, Université Paris Cité, Center for Interdisciplinary Research in Biology, Inserm, French National Centre for Scientific Research, Collège de France, Zhejiang University, Hôpital Saint-Louis, Chiba University, Sir Run Run Shaw Hospital, École Normale Supérieure - PSL, Sorbonne Université

#Nuclear Bodies #Nuclear Bodies Assembly + Show 8 more

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Abstract

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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