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Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad
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Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad
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Journal Article
Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad
2024
Overview
Membrane protein biogenesis poses acute challenges to protein homeostasis, and how they are selectively escorted to the target membrane is not well understood. Here we address this question in the guided-entry-of-tail-anchored protein (GET) pathway, in which tail-anchored membrane proteins (TAs) are relayed through an Hsp70-Sgt2-Get3 chaperone triad for targeting to the endoplasmic reticulum. We show that the Hsp70 ATPase cycle and TA substrate drive dimeric Sgt2 from a wide-open conformation to a closed state, in which TAs are protected by both substrate binding domains of Sgt2. Get3 is privileged to receive TA from closed Sgt2, whereas off-pathway chaperones remove TAs from open Sgt2. Sgt2 closing is less favorable with suboptimal GET substrates, which are rejected during or after the Hsp70-to-Sgt2 handover. Our results demonstrate how fine-tuned conformational dynamics in Sgt2 enable hydrophobic TAs to be effectively funneled onto their dedicated targeting factor while also providing a mechanism for substrate selection.
Newly synthesized tail-anchored membrane proteins (TAs) are relayed in a chaperone triad, Hsp70, Sgt2, and Get3, for delivery to the endoplasmic reticulum. Here, the authors show how the conformational dynamics of the cochaperone Sgt2 generates a decision point to enable efficient and selective TA targeting.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/80
/ 82/83
/ Carrier Proteins - metabolism
/ HSP70 Heat-Shock Proteins - metabolism
/ Humanities and Social Sciences
/ Humans
/ Membrane Proteins - metabolism
/ Molecular Chaperones - metabolism
/ Proteins
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - metabolism
/ Science
