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Substrate relay in an Hsp70-cochaperone cascade safeguards tail-anchored membrane protein targeting.

EMBO J.. 2018; 
Cho Hyunju,Shan Sh
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Peptide Synthesis Sgt2 was C-terminally labeled using Sortase-mediated ligation (Guimaraes et al, 2013). The GGGC peptide was synthesized from GenScript Primary antibodies used were anti-His tag (1:5,000, cat# A00186, GenScript), anti-Strep II tag (1:3,000, Cat# ab76949, Abcam), and anti-HA tag (1:3,000, cat#A01244, GenScript). Get A Quote

摘要

Membrane proteins are aggregation-prone in aqueous environments, and their biogenesis poses acute challenges to cellular protein homeostasis. How the chaperone network effectively protects integral membrane proteins during their post-translational targeting is not well understood. Here, biochemical reconstitutions showed that the yeast cytosolic Hsp70 is responsible for capturing newly synthesized tail-anchored membrane proteins (TAs) in the soluble form. Moreover, direct interaction of Hsp70 with the cochaperone Sgt2 initiates a sequential series of TA relays to the dedicated TA targeting factor Get3. In contrast to direct loading of TAs to downstream chaperones, stepwise substrate loading via Hsp70 ma... More

关键词

Hsp70,membrane protein biogenesis,molecular chaperone,protein aggregation,tail‐anchored prot