Journal
FEBS LETTERS
Volume 590, Issue 23, Pages 4402-4413Publisher
WILEY
DOI: 10.1002/1873-3468.12447
Keywords
crystal structure; Derlin-1; endoplasmic reticulum-associated degradation; p97; SHP motif
Funding
- National Research Foundation (NRF) [20070056157, 2013M3A9A7046297, 2013R1A2A2A01068440, 2015M2A2A4A03044653]
- National Research Foundation of Korea [2013R1A2A2A01068440, 2015M2A2A4A03044653, 2013M3A9A7046297] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Ask authors/readers for more resources
The interaction of the rhomboid pseudoprotease Derlin-1 and p97 is crucial for the retrotranslocation of polyubiquitinated substrates in the endoplasmic reticulum-associated degradation pathway. We report a 2.25 angstrom resolution structure of the p97 N-terminal domain (p97N) in complex with the Derlin-1 SHP motif. Remarkably, the SHP motif adopts a short, antiparallel -strand that interacts with the -sheet of p97Na site distinct from that to which most p97 adaptor proteins bind. Mutational and biochemical analyses contributed to defining the specific interaction, demonstrating the importance of a highly conserved binding pocket on p97N and a signature motif on SHP. Our findings may also provide insights into the interactions between other SHP-containing proteins and p97N.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available