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.
ERLIN1/2 scaffolds bridge TMUB1 and RNF170 and restrict cholesterol esterification to regulate the secretory pathway.
-
ERLIN1/ERLIN2 form large ring-like cup-shaped ER scaffolds that mediate the interaction between the full-length isoform of TMUB1 and the E3 ligase RNF170 (binding their conserved luminal N-terminal motif via the SPFH domains of adjacent ERLIN subunits); these scaffolds limit cholesterol esterification, favouring ER-to-Golgi cholesterol transport and regulating Golgi morphology and the secretory pathway. Variants that preclude these interactions have been linked to hereditary spastic paraplegia.
Biallelic variants in ERLIN1: a series of 13 individuals with spastic paraparesis.
-
Largest series to date of biallelic ERLIN1 variants (13 individuals from six families) causing SPG62 spastic paraparesis; childhood-onset, slowly progressive, predominantly pure paraparesis with possible cerebellar and peripheral-nerve involvement. Three new variants are predicted to alter the bell-shaped ring formed by the ERLIN1/ERLIN2 complex.
The Host Factor Erlin-1 is Required for Efficient Hepatitis C Virus Infection.
-
ERLIN1 is a cholesterol-binding, ER detergent-resistant-membrane protein required for efficient hepatitis C virus infection; its silencing reduces HCV RNA replication initiation, viral protein expression, and infectious virus production, acting downstream of entry and primary translation.
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
-
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.