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Park, Tae Joo
Developmental Morphogenesis Lab
Research Interests
  • Morphogenesis, chondrogenesis, ciliogenesis

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

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Title
Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway
Author
Jeong, HanbinSim, Hyo JungSong, Eun KyungLee, HakbongHa, Sung ChulJun, YoungsooPark, Tae JooLee, Changwook
Issue Date
201602
Publisher
NATURE PUBLISHING GROUP
Citation
SCIENTIFIC REPORTS, v.6, no., pp.20261 -
Abstract
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 SEL1Lcent). Strikingly, SEL1Lcent 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 SEL1Lcent 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.
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DOI
http://dx.doi.org/10.1038/srep20261
ISSN
2045-2322
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SLS_Journal Papers
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