Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER.
Blood pressure is regulated by an alpha1D-adrenergic receptor/dystrophin signalosome.
An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors.
Membrane-associated ubiquitin ligase complex containing gp78 mediates sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.
Defining human ERAD networks through an integrative mapping strategy.
Erlins restrict SREBP activation in the ER and regulate cellular cholesterol homeostasis.
A proteome-scale map of the human interactome network.
Architecture of the human interactome defines protein communities and disease networks.
Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Role of ERLINs in the Control of Cell Fate through Lipid Rafts.
Usp25-Erlin1/2 activity limits cholesterol flux to restrict virus infection.
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In human A549 cells, USP25-dependent stabilization of ERLIN1/ERLIN2 and erlin perturbations influence SREBP processing, HMGCR abundance, total cholesterol and influenza-virus output. The labeled-cholesterol efflux experiment specifically depletes ERLIN2, and the T65I mutant is ERLIN2; these are not ERLIN1-specific efflux or mutant assays.
ERLIN1/2 scaffolds bridge TMUB1 and RNF170 and restrict cholesterol esterification to regulate the secretory pathway.
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Human HeLa endogenous interactions and ERLIN1/ERLIN2 double-knockout/rescue establish erlin-complex-dependent TMUB1-L/RNF170 association. Loss of the erlins increases cholesterol esterification and perturbs Golgi morphology; SOAT1 inhibition rescues selected endpoints. Adjacent-subunit contacts and sterol-accessibility mechanisms are models, and the tested disease-analogous interface mutants are ERLIN2 constructs.
Biallelic variants in ERLIN1: a series of 13 individuals with spastic paraparesis.
The Host Factor Erlin-1 is Required for Efficient Hepatitis C Virus Infection.
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ERLIN1 depletion in human Huh-7 cells reduces establishment of HCV RNA replication and efficient infectious-particle production, while tested entry, initial translation and maintenance of established replication are less affected. The molecular step linking ERLIN1 to these viral phenotypes remains unresolved.
VCP-catalyzed ATP hydrolysis promotes the translocation of misfolded CFTR into the cytosol
RNF5 and RNF185 ubiquitinate misfolded CFTR
CFTR binds components of the ERAD machinery for ubiquitination and degradation
VCP-catalyzed ATP hydrolysis promotes the translocation of CFTR F508del into the cytosol
RNF5 and RNF185 ubiquitinate CFTR F508del
CFTR F508del binds components of the ERAD machinery for ubiquitination and degradation
Active transport of ubiquitinated CD274 from ER to cytosol
Ubiquitination of CD274 by ERAD complex
p-S195-CD274 binds ERAD complex
UniProt entry O75477 (ERLN1_HUMAN), Erlin-1 / SPFH1
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ERLIN1 is a single-pass type II ER membrane SPFH/prohibitin protein that forms the ERLIN1/ERLIN2 complex mediating ERAD of IP3 receptors, binds cholesterol, restricts SREBP activation, and interacts with the ER ubiquitin ligases AMFR/gp78, SYVN1 and (with ERLIN2) RNF170; variants cause SPG62.
SPFH1 and SPFH2 mediate the ubiquitination and degradation of inositol 1,4,5-trisphosphate receptors in muscarinic receptor-expressing HeLa cells.
RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation.