1. Structural insights into the interaction of human p97 N-terminal domain and SHP motif in Derlin-1 rhomboid pseudoprotease.
- Author
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Lim, Jia Jia, Lee, Youngjin, Yoon, So Young, Ly, Tue Tu, Kang, Jung Youn, Youn, Hyung-Seop, An, Jun Yop, Lee, Jung-Gyu, Park, Kyoung Ryoung, Kim, Tae Gyun, Yang, Jin Kuk, Jun, Youngsoo, and Eom, Soo Hyun
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PROTEOLYTIC enzymes , *UBIQUITINATION , *CHROMOSOMAL translocation , *N-terminal residues , *GENETIC mutation - Abstract
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 Å 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 β-strand that interacts with the β-sheet of p97N-a 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. [ABSTRACT FROM AUTHOR]
- Published
- 2016
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