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

• DOI: 10.1038/srep20261
• Publication Date: 2016-02-09T10:03:11Z
• Authors: Hanbin Jeong; Hyo Jung Sim; Eun Kyung Song; Hakbong Lee; Sung Chul Ha; Youngsoo Jun; Tae Joo Park; Changwook Lee
• Keywords: Endoplasmic-reticulum-associated protein degradation

Abstract Terminally misfolded proteins are selectively recognized and cleared by the endoplasmic reticulum-associated degradation (ERAD) pathway. SEL1L, a component of ERAD machinery, plays an important role in selecting transporting substrates for degradation. We have determined crystal structure mouse SEL1L central domain comprising five S el1- L ike R epeats (SLR motifs 5 to 9; hereafter called cent ). Strikingly, forms homodimer with two-fold symmetry head-to-tail manner. Particularly, SLR motif 9 dimer formation adopting domain-swapped providing extensive dimeric interface. identified that full-length self-oligomer through mammalian cells. Furthermore, we discovered SLR-C, 10 11, directly interacts N-terminus luminal loops HRD1. Therefore, propose certain play unique membrane bound machinery.