208: ZAK, Collided Ribosomes, and the Stress Switch

ZAK, Collided Ribosomes, and the Stress Switch

Music:
Enjoy the music based on this article at the end of the episode.

DOI:
10.1038/s41586-025-09772-8

License:
This episode is based on an open-access article published under the Creative Commons Attribution 4.0 International License (CC BY 4.0) – https://creativecommons.org/licenses/by/4.0/

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Episode link: https://basebybase.com/episodes/zak-collided-ribosomes-and-the-stress-switch

️ Episode:
208: ZAK, Collided Ribosomes, and the Stress Switch

️ Season:
1

Article title:
ZAK activation at the collided ribosome

Journal:
Nature

QC:
This episode was checked against the original article PDF and publication metadata for the episode release published on 2025-11-24.

QC Scope:
- article metadata and core scientific claims from the narration
- excludes analogies, intro/outro, and music
- transcript coverage: Audited the transcript’s portrayal of ZAK-RACK1 collision sensing, constitutive ribosome binding, anchor motifs (pin, ES7-patch, RIH), collision-sensing motif RIM, SAM-domain dimerization, SERBP1 competition, CLIP-seq findings, and downstream MAPK signaling.
- transcript topics: ZAK activation and constitutive ribosome binding; ZAK–RACK1 collision interface: pin, RIH, ES7/ES6 interactions; RACK1-based collision sensing via RIM FPxL motif; SAM-domain dimerization as activation switch; SERBP1 competition at RACK1 FPxL motif; CLIP-seq mapping to ES7 and ES6b/c on 18S rRNA

QC Summary:
- factual score: 10/10
- metadata score: 10/10
- supported core claims: 8
- claims flagged for review: 0
- metadata checks passed: 4
- metadata issues found: 0

Metadata Audited:
- article_doi
- article_title
- article_journal
- license

Factual Items Audited:
- ZAK activation is triggered by ribosome collisions via SAM-domain dimerization on the collision interface
- RACK1 acts as collision scaffold bridging ZAK to both collided ribosomes
- RIM FPxL motif is strictly required for ZAK activation on collided ribosomes (not binding)
- RIH motif anchors ZAK to RACK1 and is necessary for binding and activation
- SERBP1 negatively regulates ZAK by competing for the RACK1 FPxL binding site
- eS27 pin anchors ZAK to the 40S subunit via W768 and supports ribosome binding; ES7-patch also contributes

QC result: Pass.