Skip to main content
eScholarship
Open Access Publications from the University of California

A Chaperone Lid Ensures Efficient and Privileged Client Transfer during Tail-Anchored Protein Targeting.

  • Author(s): Chio, Un Seng
  • Chung, SangYoon
  • Weiss, Shimon
  • Shan, Shu-Ou
  • et al.

Published Web Location

https://doi.org/10.1016/j.celrep.2018.12.035
No data is associated with this publication.
Abstract

Molecular chaperones play key roles in maintaining cellular proteostasis. In addition to preventing client aggregation, chaperones often relay substrates within a network while preventing off-pathway chaperones from accessing the substrate. Here we show that a conserved lid motif lining the substrate-binding groove of the Get3 ATPase enables these important functions during the targeted delivery of tail-anchored membrane proteins (TAs) to the endoplasmic reticulum. The lid prevents promiscuous TA handoff to off-pathway chaperones, and more importantly, it cooperates with the Get4/5 scaffolding complex to enable rapid and privileged TA transfer from the upstream co-chaperone Sgt2 to Get3. These findings provide a molecular mechanism by which chaperones maintain the pathway specificity of client proteins in the crowded cytosolic environment.

Many UC-authored scholarly publications are freely available on this site because of the UC Academic Senate's Open Access Policy. Let us know how this access is important for you.

Item not freely available? Link broken?
Report a problem accessing this item