ArticleThe Journal of biological chemistry2009
Distinct regions within the erlins are required for oligomerization and association with high molecular weight complexes.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 40 citations in OpenAlex.
- Structures of human organellar SPFH protein complexes.Nature communications · 2025Article
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- Biallelic variants in ERLIN1: a series of 13 individuals with spastic paraparesis.Human genetics · 2024Article
- Expanding SPG18 clinical spectrum: autosomal dominant mutation causes complicated hereditary spastic paraplegia in a large family.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2024Article
- A novel autosomal dominant ERLIN2 variant activates endoplasmic reticulum stress in a Chinese HSP family.Annals of clinical and translational neurology · 2023Article
- Review
- Raft-like lipid microdomains drive autophagy initiation via AMBRA1-ERLIN1 molecular association within MAMs.Autophagy · 2021Article
- Transcriptome and Literature Mining Highlight the Differential Expression of ERLIN1 in Immune Cells during Sepsis.Biology · 2021Article
- Article
- Regulated Erlin-dependent release of the B12 transmembrane J-protein promotes ER membrane penetration of a non-enveloped virus.PLoS pathogens · 2017Article
- Assembly of Dynamic P450-Mediated Metabolons-Order Versus Chaos.Current molecular biology reports · 2017Review
- Article
- Erlins restrict SREBP activation in the ER and regulate cellular cholesterol homeostasis.The Journal of cell biology · 2013Article
- Protein-protein and protein-membrane associations in the lignin pathway.The Plant cell · 2012Article
- Characterization of the C. elegans erlin homologue.BMC cell biology · 2012Article
- Clustered hydrophobic amino acids in amphipathic helices mediate erlin1/2 complex assembly.Biochemical and biophysical research communications · 2011Article
- Quantitative proteomic analyses of human cytomegalovirus-induced restructuring of endoplasmic reticulum-mitochondrial contacts at late times of infection.Molecular & cellular proteomics : MCP · 2011Article
- The human cytomegalovirus protein UL37 exon 1 associates with internal lipid rafts.Journal of virology · 2011Article
- Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM).Biochimica et biophysica acta · 2010Review
- Cholesterol at the endoplasmic reticulum: roles of the sigma-1 receptor chaperone and implications thereof in human diseases.Sub-cellular biochemistry · 2010Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The group of stomatin/prohibitin/flotillin/HflK/C (SPFH) domain-containing proteins comprise members of diverse subcellular localization and function. Association with detergent-resistant membranes (DRMs) and the propensity to form oligomers are two common properties of SPFH domain proteins and likely important for the function of these proteins. Our laboratory recently discovered two novel members of this protein group, which, based on their endoplasmic reticulum (ER) localization and association with DRMs, were named ER lipid raft-associated protein (erlin)-1 and -2. Here we characterized erlin oligomerization and identified domains within the erlins responsible for oligomerization and DRM association. Using co-immunoprecipitation and sucrose density gradient centrifugation approaches on endogenous and ectopically expressed erlin proteins, we found that they formed homo- and hetero-oligomers and were part of large multimeric complexes. These properties were independent of their DRM association. By analyzing truncation and point mutants of erlin-2 we discovered that interaction between erlin monomers (oligomerization) and association with high molecular weight complexes require distinct regions within the protein. Although oligomerization and DRM association were mediated by a region immediately downstream of the SPFH domain (residues 228-300), integration into high molecular weight complexes was absolutely dependent on a phenylalanine residue C-terminal of this region (Phe-305), which lies within a short stretch of hydrophobic residues. Our data demonstrate that lower order oligomerization and incorporation into multimeric complexes are two separate biochemical properties of the erlins, because they are mediated by distinct regions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.