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ProteomicsAn ERAD independent role for rhomboid pseudoprotease Dfm1 in mediating sphingolipid homeostasis
Nearly one-third of nascent proteins are initially targeted to the endoplasmic reticulum (ER) where they are correctly folded and assembled before being delivered to their final cellular destinations. To prevent the accumulation of misfolded membrane proteins, ER-associated-degradation (ERAD) remove...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
MSV000090333 | MassIVE
TranscriptomicsThe ER-Associated Degradation Adapter Protein Sel1L Regulates Triglyceride Metabolism via Lipoprotein Lipase
Sel1L is an adaptor protein for the E3 ligase Hrd1 in the endoplasmic reticulum-associated degradation (ERAD), but its physiological role in a cell-type-specific manner remains unclear. Here we show that mice with adipocyte-specific Sel1L deficiency are resistant to diet-induced obesity and exhibit ...
ORGANISM(S): Mus musculus 
2015-05-18 | E-GEOD-56918 | biostudies-arrayexpress
ProteomicsCharacterization of Endoplasmic Reticulum-Associated Degradation in the human fungal pathogen C. albicans
C. albicans is the most prevalent human fungal pathogen. In immunocompromised individuals, C. albicans can cause serious systemic disease and patients infected with drug-resistant isolates have few treatment options. The Ubiquitin-Proteasome System has not been thoroughly characterized in C. albica...
ORGANISM(S): Candida Albicans (ncbitaxon:5476) 
2023-05-03 | MSV000091843 | MassIVE
TranscriptomicsSel1L is Indispensable for Mammalian ERAD, ER Homeostasis and Survival
Sel1L is an adaptor protein for the E3 ligase Hrd1 involved in endoplasmic reticulum-associated degradation (ERAD). Its physiological importance in mammalian ERAD, however, remains to be established. Here, using the inducible Sel1L knockout mouse and cell models, we provide the first in vivo evidenc...
ORGANISM(S): Mus musculus 
2013-12-04 | E-GEOD-52929 | biostudies-arrayexpress
ProteomicsHRD1 IP-MS in WT and SEL1L deficiency HEK293T cells
To gain further insights into the role and importance of SEL1L in HRD1 ERAD, we performed unbiased proteomics LC-MS analyses to map SEL1L and HRD1 interactomes in WT and SEL1L-/-, WT and HRD1-/- HEK293T cells, respectively.
ORGANISM(S): Homo sapiens (Human) 
2024-01-10 | PXD043674 | Pride
Erad complex formation Sel1l-hrd1 erad Hek293t 
ProteomicsRegulation of hepatic inclusions and fibrinogen biogenesis by SEL1L-HRD1 ERAD
Impaired secretion of an essential blood coagulation factor fibrinogen leads to hepatic fibrinogen storage disease (HFSD), characterized by the presence of fibrinogen-positive inclusion bodies and hypofibrinogenemia. However, the molecular mechanisms underlying the biogenesis of fibrinogen in the en...
ORGANISM(S): Mus musculus (Mouse) 
2024-09-11 | PXD047658 | Pride
Hepatocytes Sel1l-hrd1 erad Fibrinogen Inclusion bodies 
UnknownConserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex formation for ER-associated degradation (ERAD).
Not available
S-EPMC5665440 | biostudies-literature
UnknownDerlin-3 Is Required for Changes in ERAD Complex Formation under ER Stress.
Not available
S-EPMC7504720 | biostudies-literature
UnknownSEL1L-HRD1 interaction is required to form a functional HRD1 ERAD complex.
Not available
S-EPMC10873344 | biostudies-literature
UnknownStructural basis and pathological implications of the dimeric OS9-SEL1L-HRD1 ERAD Core Complex.
Not available
S-EPMC12949252 | biostudies-literature
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