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/ Support:Base by Base – Stripe donations: https://donate.stripe.com/7sY4gz71B2sN3RWac5gEg00 Official website https://basebybase.com On PaperCast Base by Base you’ll discover the latest in genomics, functional genomics, structural genomics, and proteomics. 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. Chapters (00:00:00) - The cell's ribotoxic stress response(00:05:10) - The Rack 1 Collapse Sensor(00:09:55) - How does the ZK SAM domains dimerize to trigger cell(00:12:16) - When We Collide