Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells.

Ribosome stalling triggers the ribosome-associated quality control pathway, which targets collided ribosomes and leads to subunit dissociation, followed by proteasomal degradation of the nascent peptide. In yeast, is triggered by Hel2-dependent ubiquitination of uS10, followed by subunit dissociation mediated by the complex. In mammals, ZNF598-dependent ubiquitination of collided ribosomes is required for and activating signal cointegrator 3 (ASCC3), a component of the ASCC complex, facilitates However, the roles of other components and associated factors of the ASCC complex remain unknown. Here, we demonstrate that the human duanyu1745C-trigger complex, an ortholog of the yeast complex, plays crucial roles in duanyu1745C. The complex is composed of ASCC3, ASCC2, and TRIP4, which are orthologs of the RNA helicase Slh1(Rqt2), ubiquitin-binding protein Cue3(Rqt3), and zinc-finger type protein yKR023W(Rqt4), respectively. The ATPase activity of ASCC3 and the ubiquitin-binding activity of ASCC2 are crucial for triggering duanyu1745C. Given the proposed function of the duanyu1745T complex in yeast, we propose that the hduanyu1745T complex recognizes the ubiquitinated stalled ribosome and induces subunit dissociation to facilitate

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