Structure of the E3 ligase CRL2ZYG11B with substrates reveals the molecular basis for N-degron recognition and ubiquitination.

Xi Liu; Y Li; Lennice K. Castro; Zanlin Yu; Yifan Cheng; Matthew D. Daugherty; John D. Gross

doi:10.1016/j.celrep.2026.117401

June 1, 2026

Structure of the E3 ligase CRL2ZYG11B with substrates reveals the molecular basis for N-degron recognition and ubiquitination.

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Key Points

This research investigates how the E3 ligase complex CRL2 ZYG11B recognizes Gly/N-degron substrates.
Analyzed the structure of CRL2 ZYG11B with its substrates.
Investigated the role of viral protease in NLRP1 inflammasome activation.
Demonstrated how the structure of CRL2 ZYG11B aids in Gly/N-degron substrate recognition.
Revealed mechanisms for ubiquitination impacting inflammasome activity.

Implication

Examines N-degron recognition and ubiquitination in substrates, indicating mechanisms of inflammasome activation.

Abstract

E3 ligase complex recognizes Gly/N-degron substrates, including those that are involved in viral protease-mediated activation of the NLRP1 inflammasome.

Discussion

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Cite This Study

Liu et al. (2026) studied this question.

synapsesocial.com/papers/6a21151ad499ed480b16e618 https://doi.org/10.1016/j.celrep.2026.117401

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Structure of the E3 ligase CRL2ZYG11B with substrates reveals the molecular basis for N-degron recognition and ubiquitination.

Key Points

Implication

Abstract

Discussion

Cite This Study

Structure of the E3 ligase CRL2ZYG11B with substrates reveals the molecular basis for N-degron recognition and ubiquitination.

Key Points

Implication

Abstract

Discussion

Cite This Study

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