ArticleScientific reports2016
Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- Natural SEL1L variants rescue a model of NGLY1 deficiency and modify ERAD function and proteasome sensitivity.PLoS genetics · 2025Article
- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- TTC17 is an endoplasmic reticulum resident TPR-containing adaptor protein.The Journal of biological chemistry · 2023Article
- Protein quality control and aggregation in the endoplasmic reticulum: From basic to bedside.Frontiers in cell and developmental biology · 2023Review
- Identification of novel genes for triple-negative breast cancer with semiparametric gene-based analysis.Journal of applied statistics · 2023Article
- Augmented ERAD (ER-associated degradation) activity in chondrocytes is necessary for cartilage development and maintenance.Science advances · 2022Article
- Article
- Endoplasmic Reticulum Quality Control in Immune Cells.Frontiers in cell and developmental biology · 2021Review
- A decade of research on the second messenger c-di-AMP.FEMS microbiology reviews · 2020Review
- Functional Innovation in the Evolution of the Calcium-Dependent System of the Eukaryotic Endoplasmic Reticulum.Frontiers in genetics · 2020Article
- Disruption of valosin-containing protein activity causes cardiomyopathy and reveals pleiotropic functions in cardiac homeostasis.The Journal of biological chemistry · 2019Article
- TPR-containing proteins control protein organization and homeostasis for the endoplasmic reticulum.Critical reviews in biochemistry and molecular biology · 2019Review
- Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex formation for ER-associated degradation (ERAD).Journal of cell science · 2017Article
- Article
- New Insights into the Physiological Role of Endoplasmic Reticulum-Associated Degradation.Trends in cell biology · 2017Review
- Varicella-Zoster Virus Infectious Cycle: ER Stress, Autophagic Flux, and Amphisome-Mediated Trafficking.Pathogens (Basel, Switzerland) · 2016Review
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 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.
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