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<p>Proteasomes degrade diverse proteins in different cellular contexts through incompletely defined regulatory mechanisms. Here we report the cryo-EM structure of human thioredoxin-like protein 1 (TXNL1) bound to the 19S regulatory particle of proteasomes via interactions with PSMD1 (Rpn2), PSMD4 (Rpn10) and PSMD14 (Rpn11). Proteasome binding is necessary for the ubiquitin-independent degradation of TXNL1 upon cellular exposure to metal- or metalloid-containing oxidative agents, thereby establishing a structural requirement for the stress-induced degradation of TXNL1.</p>

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Structure of the TXNL1-bound proteasome

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2025年8月6日

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  • Jingjing Gao,
  • Christopher Nardone,
  • Matthew C. J. Yip,
  • Haruka Chino,
  • Xin Gu,
  • Zachary Mirman,
  • Michael J. Rale,
  • Joao A. Paulo,
  • Stephen J. Elledge,
  • Sichen Shao

摘要

Proteasomes degrade diverse proteins in different cellular contexts through incompletely defined regulatory mechanisms. Here we report the cryo-EM structure of human thioredoxin-like protein 1 (TXNL1) bound to the 19S regulatory particle of proteasomes via interactions with PSMD1 (Rpn2), PSMD4 (Rpn10) and PSMD14 (Rpn11). Proteasome binding is necessary for the ubiquitin-independent degradation of TXNL1 upon cellular exposure to metal- or metalloid-containing oxidative agents, thereby establishing a structural requirement for the stress-induced degradation of TXNL1.