Ask about this productRelated genes to: ERLIN2 Blocking Peptide
- Gene:
- ERLIN2 NIH gene
- Name:
- ER lipid raft associated 2
- Previous symbol:
- C8orf2, SPFH2, SPG18
- Synonyms:
- NET32, Erlin-2
- Chromosome:
- 8p11.23
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-03
- Date modifiied:
- 2019-04-23
Related products to: ERLIN2 Blocking Peptide
Related articles to: ERLIN2 Blocking Peptide
- Extracellular vesicles (EVs) isolated from tumor tissues carry disease-associated proteins and surface antigens, making them promising candidates for cancer diagnostics and immunotherapy. For EV-based approaches to reach clinical application, it is essential that functional EVs can be obtained from clinically accessible materials, including cryopreserved tumor tissues stored in biobanks. Whether cryopreservation alters EV integrity and function remains unclear. This study evaluates whether EVs derived from cryopreserved tumor tissues retain key molecular and biological properties required for diagnostic and therapeutic use. - Source: PubMed
Publication date: 2026/05/21
D Arrigo DanielePark Kyong-SuLässer CeciliaSigalas Georgios PanagiotisSymonds EmmaUrzí OrnellaLocatelli CamillaOlofsson Bagge RogerLötvall JanCrescitelli Rossella - Hepatocellular carcinoma (HCC) ranks among the most lethal cancers, and its dismal prognosis underscores the urgent need to elucidate the underlying carcinogenic mechanisms. Endoplasmic reticulum lipid rafts associated protein 2 (ERLIN2), an endoplasmic reticulum protein, has been implicated in various malignant tumors. However, its functional role in HCC remains poorly understood. Here, we found elevated ERLIN2 expression and N-glycosylation modification at asparagine 106 (N106) in HCC. We identify site-specific N-glycosylation as a crucial advantage of ERLIN2 that may result in aberrant cancer cell growth. Overexpression of either N-glycosylated ERLIN2 (wild-type, WT) or an asparagine-to-glutamine mutant (N106Q) in HCC cell lines indicated that N106 N-glycosylation of ERLIN2 acts as an important advantage in the tumorigenesis and triggers aberrant cell proliferation, migration, and invasion. Furthermore, we found that E3 ubiquitin ligase membrane-associated ring-CH-type finger protein 6 (MARCHF6) can mediate the ubiquitination degradation of ERLIN2, and this effect is more significant after the N-glycosylation at the N106 site is inhibited. In addition, excessive N-glycosylation at this site enhanced the interaction between ERLIN2 and cyclin B1 (CCNB1), leading to dysregulated CCNB1 expression and further accelerating the progression of HCC. Comprehensive studies confirm that N-glycosylation is a significant post-translational modification of ERLIN2 in HCC, and elucidating this mechanism may pave the way for the development of novel therapeutic strategies in the future. - Source: PubMed
Publication date: 2026/05/21
Li SijieHuang HuanhuanFeng JiahuiGu QiangSun Daquan - Mitochondrial DNA replication occurs at contact sites between the endoplasmic reticulum (ER) and mitochondria (ERMCS). Beyond the known role of the tubular ER protein RTN4, the factors regulating this process are poorly defined. Here, we show that repressing the ER protein ERLIN2 in human fibroblasts depletes ER-mitochondrial contact sites and inhibits mitochondrial DNA replication, as does silencing RTN4 or the ER-mitochondrial tether GRP75. GRP75 or RTN4 scarcity also decreases the level of the mitochondrial calcium uniporter (MCU), whose inhibition blocks mitochondrial DNA synthesis. Because ERMCS depletion did not diminish mitochondrial calcium, and MCU complex can transport manganese, we tested whether manganese could bypass these defects. Manganese supplementation restored mitochondrial DNA replication in cells lacking ERMCS or with inhibited MCU, identifying manganese as a critical mediator. We then considered mitochondrial transcription as a potential manganese target, since it provides both transcripts for gene expression and primers for DNA replication. In vitro, manganese inhibits transcription re-start and stimulates RNA synthesis at the light-strand origin of replication. These findings support a model in which ER-mitochondrial contact sites, in conjunction with MCU, deliver manganese from the ER to mitochondria to promote DNA replication, potentially by modulating mitochondrial RNA polymerase activity. - Source: PubMed
Lopez de Arbina AmaiaZamudio-Ochoa AngelicaMuñoz-Oreja MikelPerez-Rodriguez DiegoMosqueira-Martín LauraLasalandra RebeccaVillar-Fernandez MarinaFernandez-Pelayo UxoaRodriguez-Gomez LauraLee SeungtaeGil-Bea FranciscoOsinalde NereaVallejo-Illaramendi AinaraTemiakov DmitrySpinazzola AntonellaHolt Ian J - This study aims to explore the potential molecular mechanisms by which di (2-ethylhexyl) phthalate (DEHP) exposure induces pulmonary arterial hypertension (PAH). - Source: PubMed
Publication date: 2026/03/20
Li HuaJiang YingchunLi Jijia - The SPFH (stomatin, prohibitin, flotillin, and HflK/C) family proteins are proposed scaffolds for organizing functional membrane microdomains (FMMs) on various cellular membranes. Erlin1 and Erlin2, two endoplasmic reticulum (ER)-residing SPFH members, as heteromeric complexes, participate in ER-associated protein degradation (ERAD). However, the mechanisms underlying Erlin-mediated FMM organization and ERAD regulation remain poorly understood. Here, through cryoelectron microscopy (cryo-EM), we find that the human Erlin1/2 complex forms a 26-mer cage assembly, defining a nanometer-sized microdomain on the luminal leaflet. The intramembrane region of each subunit constitutes a specific phosphatidylinositol-binding pocket. ER proteins can be recruited to both the interior and exterior of these cages. By caging cargoes, the Erlin1/2 complex physically secludes them from their substrates or binding partners, conferring another layer of regulation on their functions. Moreover, individual cages can cluster to organize FMMs of different sizes. These dynamic properties underscore a general regulatory role of Erlin1/2 in various ER-related biological processes, including coronaviral replication. - Source: PubMed
Publication date: 2026/03/25
Yan LuXu ZihongYao YuanhangAwang TadsaneeWang XiaotingWang YonglunMa ChengyingLi NingningSong ChenChen Xiao-WeiGao Ning