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Sel-1 suppressor of lin-12-like

SEL1L, IBD2, SEL1-like
The protein encoded by this gene is part of a protein complex required for the retrotranslocation or dislocation of misfolded proteins from the endoplasmic reticulum lumen to the cytosol, where they are degraded by the proteasome in a ubiquitin-dependent manner. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2011] (from NCBI)
Top mentioned proteins: HRD1, Ethanolaminephosphotransferase, Ubiquitin, IBD, OS-9
Papers on SEL1L
Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-L.
Wada et al., Kyoto, Japan. In Febs J, Jan 2016
Mammalian HRD1, an integral membrane ubiquitin ligase that ubiquitinates ERAD substrates, forms a large assembly in the ER membrane including SEL1L, a single-pass membrane protein, and additional components.
Epithelial Sel1L is required for the maintenance of intestinal homeostasis.
Qi et al., South Brisbane, Australia. In Mol Biol Cell, Jan 2016
Here we show that the expression of SEL1L and HRD1, the most conserved branch of mammalian ERAD, is significantly reduced in ileal Crohn's disease (CD).
IRE1α is an endogenous substrate of endoplasmic-reticulum-associated degradation.
Qi et al., Ithaca, United States. In Nat Cell Biol, Dec 2015
Here we discover that IRE1α, the sensor of the unfolded protein response (UPR), is a bona fide substrate of the Sel1L-Hrd1 ERAD complex.
Identifying the ERAD ubiquitin E3 ligases for viral and cellular targeting of MHC class I.
Lehner et al., Cambridge, United Kingdom. In Mol Immunol, Dec 2015
Free US11 either rebinds more MHC-I or is itself degraded by the HRD1/SEL1L E3 ligase complex.
Metabolomic Quantitative Trait Loci (mQTL) Mapping Implicates the Ubiquitin Proteasome System in Cardiovascular Disease Pathogenesis.
Shah et al., Durham, United States. In Plos Genet, Nov 2015
Our strongest findings were for SCDA metabolite levels with variants in genes that regulate components of endoplasmic reticulum (ER) stress (USP3, HERC1, STIM1, SEL1L, FBXO25, SUGT1) These findings were validated in a second cohort of CATHGEN subjects (N = 2022, combined p = 8.4x10-6-2.3x10-10).
PDI reductase acts on Akita mutant proinsulin to initiate retrotranslocation along the Hrd1/Sel1L-p97 axis.
Tsai et al., Ann Arbor, United States. In Mol Biol Cell, Nov 2015
Here we establish key ERAD machinery components used to triage the Akita proinsulin mutant, including the Hrd1-Sel1L membrane complex, which conducts Akita proinsulin from the ER lumen to the cytosol, and the p97 ATPase, which couples the cytosolic arrival of proinsulin with its proteasomal degradation.
Endoplasmic reticulum quality control in cancer: Friend or foe.
Qi et al., Ithaca, United States. In Semin Cancer Biol, Aug 2015
Here we review recent advances in our understanding of the complex relationship between ER proteostasis and cancer pathology, with a focus on the two most conserved ER quality-control mechanisms--the IRE1α-XBP1 pathway of the UPR and SEL1L-HRD1 complex of the ERAD.
Virus-encoded microRNA contributes to the molecular profile of EBV-positive burkitt lymphomas.
Leoncini et al., Bologna, Italy. In Oncotarget, Aug 2015
Among others, we identified LIN28B, CGNL1, GCET2, MRAS, PLCD4, SEL1L, SXX1, and the tyrosine kinases encoding STK10/STK33, all provided with potential pathogenetic significance.
A CRISPR-Based Screen Identifies Genes Essential for West-Nile-Virus-Induced Cell Death.
Wu et al., El Paso, United States. In Cell Rep, Aug 2015
Among the genes identified, seven genes, EMC2, EMC3, SEL1L, DERL2, UBE2G2, UBE2J1, and HRD1, stood out as having the strongest phenotype, whose knockout conferred strong protection against WNV-induced cell death with two different WNV strains and in three cell lines.
The ER-associated degradation adaptor protein Sel1L regulates LPL secretion and lipid metabolism.
Qi et al., Ithaca, United States. In Cell Metab, 2014
Sel1L is an essential adaptor protein for the E3 ligase Hrd1 in the endoplasmic reticulum (ER)-associated degradation (ERAD), a universal quality-control system in the cell; but its physiological role remains unclear.
How viruses hijack the ERAD tuning machinery.
Molinari et al., Bellinzona, Switzerland. In J Virol, 2014
Recent reports highlight the analogies between mouse hepatitis virus-, equine arteritis virus-, and Japanese encephalitis virus-induced replication platforms and ER-associated degradation (ERAD) tuning vesicles (or EDEMosomes) that display nonlipidated LC3 at their cytosolic face and segregate the ERAD factors EDEM1, OS-9, and SEL1L from the ER lumen.
A single-nucleotide polymorphism in tumor suppressor gene SEL1L as a predictive and prognostic marker for pancreatic ductal adenocarcinoma in Caucasians.
Frazier et al., Houston, United States. In Mol Carcinog, 2012
the rs12435998 SNP in SEL1L gene plays a role in modifying age at diagnosis of PDA in Caucasian nonsmokers.
SEL1L, an UPR response protein, a potential marker of colonic cell transformation.
Biunno et al., Washington, D.C., United States. In Dig Dis Sci, 2012
SEL1L expression is a potential colorectal cancer (CRC) tissue biomarker since its expression is significantly higher in adenoma cells with respect to normal mucosa; the levels of expression decrease in undifferentiated CRC cancers
Haploid insufficiency of suppressor enhancer Lin12 1-like (SEL1L) protein predisposes mice to high fat diet-induced hyperglycemia.
Long et al., Ithaca, United States. In J Biol Chem, 2011
a critical and previously unknown function for SEL1L in regulating adult beta-cell function and growth
mSEL-1L (Suppressor/enhancer Lin12-like) protein levels influence murine neural stem cell self-renewal and lineage commitment.
Biunno et al., Milano, Italy. In J Biol Chem, 2011
mSEL-1L as a primitive marker with a possible involvement in the regulation of neural progenitor stemness maintenance and lineage determination.
SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates.
Hosokawa et al., Kyoto, Japan. In J Biol Chem, 2011
regulation of the stability and assembly of the HRD1-SEL1L complex is critical to optimize the degradation kinetics of ERAD substrates
The role of MRH domain-containing lectins in ERAD.
Kato et al., Kyoto, Japan. In Glycobiology, 2010
Recent studies have determined that both OS-9 and XTP3-B are ER resident proteins that associate with the HRD1-SEL1L ubiquitin ligase complex and are important for the regulation of ERAD.
Mannose 6-phosphate receptor homology domain-containing lectins in mammalian endoplasmic reticulum-associated degradation.
Kamiya et al., Kyoto, Japan. In Methods Enzymol, 2009
Furthermore, these lectins associate with the HRD1-SEL1L ubiquitin ligase complex on the ER membrane.
OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD.
Kopito et al., Stanford, United States. In Nat Cell Biol, 2008
OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells.
Helenius et al., Zürich, Switzerland. In Cell, 2007
We analyzed the effects of ER-associated processes and factors on infection and on isolated viruses and found that SV40 makes use of the thiol-disulfide oxidoreductases, ERp57 and PDI, as well as the retrotranslocation proteins Derlin-1 and Sel1L.
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