Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway.

Citation data:

Scientific reports, ISSN: 2045-2322, Vol: 6, Issue: 1, Page: 20261

Publication Year:
2016
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Repository URL:
http://scholarworks.unist.ac.kr/handle/201301/18750
PMID:
27064360
DOI:
10.1038/srep20261
PMCID:
PMC4746701
Author(s):
Jeong, Hanbin; Sim, Hyo Jung; Song, Eun Kyung; Lee, Hakbong; Ha, Sung Chul; Jun, Youngsoo; Park, Tae Joo; Lee, Changwook
Publisher(s):
Springer Nature; NATURE PUBLISHING GROUP
Tags:
Multidisciplinary
article description
Terminally misfolded proteins are selectively recognized and cleared by the endoplasmic reticulum-associated degradation (ERAD) pathway. SEL1L, a component of the ERAD machinery, plays an important role in selecting and transporting ERAD substrates for degradation. We have determined the crystal structure of the mouse SEL1L central domain comprising five Sel1-Like Repeats (SLR motifs 5 to 9; hereafter called SEL1L(cent)). Strikingly, SEL1L(cent) forms a homodimer with two-fold symmetry in a head-to-tail manner. Particularly, the SLR motif 9 plays an important role in dimer formation by adopting a domain-swapped structure and providing an extensive dimeric interface. We identified that the full-length SEL1L forms a self-oligomer through the SEL1L(cent) domain in mammalian cells. Furthermore, we discovered that the SLR-C, comprising SLR motifs 10 and 11, of SEL1L directly interacts with the N-terminus luminal loops of HRD1. Therefore, we propose that certain SLR motifs of SEL1L play a unique role in membrane bound ERAD machinery.