Affinage

ERLIN2

Erlin-2 · UniProt O94905

Length
339 aa
Mass
37.8 kDa
Annotated
2026-06-09
36 papers in source corpus 20 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ERLIN2 (erlin-2/SPFH2) is an ER membrane protein that, together with erlin-1, assembles into a large ring/cage-shaped hetero-oligomeric complex (~2 MDa, a 26-mer of alternating erlin-1/erlin-2 subunits) that organizes lipid-raft-like microdomains on the ER and physically sequesters cargo proteins from their binding partners [PMID:19240031, PMID:bio_10.1101_2025.04.21.649849, PMID:bio_10.1101_2025.06.14.659634]. It resides in detergent-resistant, cholesterol-dependent ER membrane fractions, with its extreme N-terminus directing ER targeting (PMID:16835267). A central function of the complex is substrate recognition in ER-associated degradation (ERAD): erlin-2 (the dominant IP3R-binding subunit) associates with activated IP3R tetramers prior to their polyubiquitination and p97 recruitment, and is required for IP3R ubiquitination and proteasomal degradation while leaving calcium mobilization intact (PMID:17502376, PMID:19240031, PMID:19751772, PMID:30135210). The erlin-1/2 complex directly and selectively binds phosphatidylinositol 3-phosphate (PI(3)P) through determinants within erlin-2, and this PI(3)P binding stabilizes cellular PI(3)P pools to sustain autophagic flux without altering VPS34 kinase activity or endocytosis (PMID:30135210, PMID:39018973). Beyond ERAD, ERLIN2 participates in lipid and sterol regulation by binding INSIG1 to promote SREBP1c activation and lipid droplet accumulation (PMID:22690709), cooperating with CLPTM1L to stabilize SREBP1 by inhibiting its ubiquitination (PMID:40550808), and facilitating StAR-mediated cholesterol transport from the ER to mitochondria via MAM contact sites (PMID:41251286). ERLIN2 also stabilizes Cyclin B1 through K63-linked ubiquitination during G2/M, associating with α-tubulin and the Cyclin B1/Cdk1 complex such that its loss causes cell cycle arrest (PMID:27462423), and it regulates IP3R-mediated Ca2+ release that activates CaMKII-MAPK-CREB signaling to maintain circadian rhythmicity (PMID:41572931). Disease-linked ERLIN2 variants (T65I and V71A) impair erlin-2–IP3R interaction, PI(3)P binding, and calcium homeostasis, linking ERLIN2 dysfunction to spastic paraplegia and motor neuron disease (PMID:30135210, PMID:40225166, PMID:37752894).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2006 High

    Established where ERLIN2 acts and how it is targeted, defining it as a cholesterol-dependent, lipid-raft-associated ER membrane protein.

    Evidence Sucrose gradient fractionation, cholesterol depletion, and GFP-fusion targeting assays in multiple cell types

    PMID:16835267

    Open questions at the time
    • Function of the raft-like microdomain not yet defined
    • No binding partners identified at this stage
  2. 2007 High

    Answered what ERLIN2 does mechanistically by showing it acts as an ERAD substrate-recognition factor that engages activated IP3Rs before their ubiquitination.

    Evidence Co-immunoprecipitation, siRNA knockdown, and pulse-chase degradation assays

    PMID:17502376

    Open questions at the time
    • E3 ligase and how recognition triggers ubiquitination unknown
    • Whether ERLIN2 acts alone or in a complex unresolved
  3. 2009 High

    Resolved that ERLIN2 functions within a large erlin-1/erlin-2 ring complex required for IP3R ERAD, defining the structural unit and its substrate selectivity.

    Evidence Co-IP, sucrose gradient sedimentation, EM of native complex, RNAi, and substrate-specificity controls (no effect on HMG-CoA reductase or IκBα)

    PMID:19240031 PMID:19751772

    Open questions at the time
    • Atomic stoichiometry not yet determined
    • How the complex distinguishes activated from inactive IP3R unknown
  4. 2012 Medium

    Extended ERLIN2 function beyond IP3R ERAD to membrane-protein complexes and lipid metabolism, including γ-secretase association, ER-stress cytoprotection, and INSIG1-dependent SREBP1c activation.

    Evidence Affinity purification/MS, PLA, Co-IP, RNAi with Aβ/Notch readouts; ER-stress gain/loss-of-function; INSIG1 Co-IP with lipid droplet and SREBP1c assays

    PMID:22681620 PMID:22690709 PMID:22771797

    Open questions at the time
    • Each link reported from a single lab
    • Mechanistic relationship between ERAD role and lipid/secretase functions unclear
  5. 2015 Medium

    Showed ERLIN2 has a cell-cycle role distinct from degradation, stabilizing Cyclin B1 via K63-linked ubiquitination at the ER-microtubule interface.

    Evidence Reciprocal Co-IP (α-tubulin, Cyclin B1/Cdk1), K63-linkage-specific ubiquitination assay, FACS cell-cycle analysis, siRNA

    PMID:27462423

    Open questions at the time
    • E3 ligase mediating K63 ubiquitination not identified
    • How a degradation-associated factor switches to stabilization unexplained
  6. 2018 High

    Defined ERLIN2 as the dominant IP3R- and PI(3)P-binding subunit and linked a disease mutation (T65I) mechanistically to loss of both interactions.

    Evidence CRISPR ablation of erlin-1 or erlin-2, PI(3)P lipid-binding assays, Co-IP, ubiquitination assay, T65I mutagenesis

    PMID:30135210

    Open questions at the time
    • Structural basis of the PI(3)P-binding site not resolved
    • Functional consequence of PI(3)P binding not yet established
  7. 2021 Medium

    Broadened ERLIN2's ERAD substrate repertoire to the WNT secretory factor EVI/WLS and connected it to specific E2 enzymes independent of canonical ER E3 ligases.

    Evidence RNAi screen, Co-IP, ubiquitin-linkage-specific antibodies, E2/E3 knockdown

    PMID:34406391

    Open questions at the time
    • The E3 ligase for EVI/WLS not identified
    • Single-lab finding
  8. 2024 High

    Linked ERLIN2's PI(3)P binding to a physiological output, showing the complex stabilizes cellular PI(3)P pools to sustain autophagic flux.

    Evidence In vitro PI(3)P binding with recombinant erlins, PI(3)P quantification in KO/disrupted cells, autophagic flux assay, VPS34 activity measurement

    PMID:39018973

    Open questions at the time
    • Molecular mechanism by which bound PI(3)P is protected from turnover unknown
    • Single-lab study
  9. 2025 High

    Provided the atomic architecture of the complex, defining it as a 26-mer cage that sequesters cargo and oligomerizes into membrane microdomains.

    Evidence Two independent single-particle cryo-EM studies under multiple detergent conditions (preprints)

    PMID:bio_10.1101_2025.04.21.649849 PMID:bio_10.1101_2025.06.14.659634

    Open questions at the time
    • Structures of cargo-bound complex not resolved
    • Preprint status, not peer-reviewed
  10. 2025 Medium

    Added sterol-trafficking and SREBP1-stabilization roles, showing ERLIN2 chaperones StAR folding for ER-to-mitochondria cholesterol transport and cooperates with CLPTM1L to stabilize SREBP1.

    Evidence Co-IP (ERLIN2-StAR at ER/MAM; CLPTM1L-ERLIN2), KO/knockdown, mitochondrial cholesterol transport and SREBP1 ubiquitination assays

    PMID:40550808 PMID:41251286

    Open questions at the time
    • How a cage/sequestration function relates to folding chaperone activity unclear
    • Single-lab findings
  11. 2026 Medium

    Connected ERLIN2-regulated IP3R Ca2+ signaling to downstream circadian control and defined post-translational regulation of ERLIN2 itself.

    Evidence C2C12 circadian reporter and Ca2+ imaging with IP3R/CaMKII/MAPK inhibition; N106Q mutagenesis, MARCHF6 knockdown/overexpression, CCNB1 Co-IP

    PMID:41572931 PMID:42166002

    Open questions at the time
    • Whether circadian role generalizes beyond skeletal muscle untested
    • Single-lab findings
  12. 2023 Medium

    Tied ERLIN2 dysfunction to human disease through patient-derived variants that disrupt IP3R handling and ER homeostasis.

    Evidence Patient iPSC models, IP-MS identifying RNF213 recruitment to IP3R1, Ca2+ imaging, MAPK analysis, ER morphology imaging, neuronal axon assays

    PMID:37752894 PMID:40225166

    Open questions at the time
    • Variant V71A studied in single labs
    • How aberrant RNF213 recruitment relates to normal ERAD pathway unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the single cage complex integrates its diverse roles — ERAD substrate selection, PI(3)P stabilization, sterol trafficking, and Cyclin B1 stabilization — into a coherent regulatory logic remains unresolved.
  • No unifying model linking cargo sequestration to the multiple downstream pathways
  • Identity of E3 ligases for several substrates unknown
  • Structural basis for substrate vs. lipid selectivity undetermined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 3 GO:0140096 catalytic activity, acting on a protein 3 GO:0008289 lipid binding 2 GO:0044183 protein folding chaperone 1
Localization
GO:0005783 endoplasmic reticulum 3
Pathway
R-HSA-392499 Metabolism of proteins 4 R-HSA-1430728 Metabolism 3 R-HSA-1640170 Cell Cycle 3 R-HSA-9612973 Autophagy 1 R-HSA-9909396 Circadian clock 1
Partners
CCNB1CLPTM1LERLIN1INSIG1ITPR1KCNN1MARCHF6STARD1
Complex memberships
erlin-1/erlin-2 (SPFH1/SPFH2) cage complex

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2006 Erlin-2 (C8orf2) localizes to the ER membrane and is enriched in detergent-insoluble, buoyant (lipid-raft-like) fractions in a cholesterol-dependent manner. The extreme N-terminus is sufficient for ER targeting in the absence of classical ER retrieval motifs. Sucrose gradient fractionation, cholesterol depletion, GFP-fusion subcellular targeting assay, monoclonal antibody generation Journal of cell science High 16835267
2007 SPFH2 (ERLIN2) rapidly associates with activated IP3Rs prior to their polyubiquitination and p97 recruitment, and RNAi-mediated suppression of SPFH2 markedly inhibits IP3R polyubiquitination and degradation as well as the processing of other ERAD substrates, identifying ERLIN2 as a key ERAD substrate recognition factor. Co-immunoprecipitation, RNA interference (siRNA knockdown), pulse-chase degradation assay The Journal of biological chemistry High 17502376
2009 SPFH1 (erlin-1) and SPFH2 (erlin-2) form a heteromeric ~2 MDa ring-shaped complex (diameter ~250 Å) that binds to IP3R tetramers immediately after their activation and is required for their polyubiquitination and degradation; RNAi depletion of either subunit blocks IP3R ERAD. Co-immunoprecipitation, sucrose gradient sedimentation, electron microscopy of native complex, RNA interference The Journal of biological chemistry High 19240031
2009 SPFH1/SPFH2 (erlin-1/erlin-2) hetero-oligomeric complex associates with IP3Rs after their activation but before polyubiquitination and p97 association, selectively mediating IP3R ERAD but not HMG-CoA reductase sterol-induced ERAD; suppression of both subunits inhibits IP3R polyubiquitination and degradation without affecting IP3R-mediated calcium mobilization. Stable m3 muscarinic receptor-expressing HeLa cells, co-immunoprecipitation, RNA interference, calcium mobilization assay, IκBα processing assay as negative control Biochimica et biophysica acta High 19751772
2012 Erlin-2 physically associates with active γ-secretase in detergent-resistant ER membranes (DRMs) of brain, and siRNA knockdown of erlin-2 reduces Aβ production with limited effect on Notch processing, identifying erlin-2 as a γ-secretase-associated protein (GSAP) that affects APP substrate selectivity. γ-secretase inhibitor affinity purification, tandem mass spectrometry, proximity ligation assay, co-immunoprecipitation, siRNA knockdown with Aβ and Notch processing readouts Biochemical and biophysical research communications Medium 22771797
2012 ERLIN2 overexpression promotes breast cancer cell survival and adaptation to ER stress; IRE1α/XBP1 axis modulates ERLIN2 protein levels; gain- and loss-of-function show ERLIN2 facilitates cytoprotective response to ER stress. Stable overexpression (pLenti6/V5-ERLIN2), RNAi knockdown, ER stress induction assays, IRE1α inhibition BMC cancer Medium 22681620
2012 ERLIN2 binds to INSIG1 at the ER membrane and promotes SREBP1c activation, leading to increased cytosolic lipid droplet accumulation; ERLIN2 expression is induced by insulin signaling or lipoprotein-deficient medium. Co-immunoprecipitation (ERLIN2–INSIG1 binding), siRNA knockdown, lipid droplet quantification, SREBP1c activation assays The Biochemical journal Medium 22690709
2015 ERLIN2 acts as an ER-microtubule-binding protein that interacts with α-tubulin and simultaneously binds the Cyclin B1/Cdk1 mitosis-promoting complex during G2/M phase; ERLIN2 facilitates K63-linked ubiquitination and stabilization of Cyclin B1, and its downregulation causes cell cycle arrest. Co-immunoprecipitation (ERLIN2–α-tubulin and ERLIN2–Cyclin B1/Cdk1), ubiquitination assay (K63-linkage specific), cell cycle analysis (FACS), siRNA knockdown Cell discovery Medium 27462423
2018 Erlin2 is the dominant mediator of IP3R binding within the erlin1/2 complex; the disease-linked T65I mutation (spastic paraplegia) dramatically inhibits erlin2–IP3R interaction and IP3R ubiquitination/degradation. The erlin1/2 complex specifically binds phosphatidylinositol 3-phosphate (PI(3)P), erlin2 binds PI(3)P much more strongly than erlin1, and the T65I mutation inhibits this PI(3)P binding; multiple determinants within the erlin2 polypeptide comprise the PI(3)P-binding site. Gene editing (CRISPR ablation of erlin1 or erlin2), PI(3)P lipid-binding assay, co-immunoprecipitation (erlin2–IP3R), ubiquitination assay, T65I mutant functional analysis The Journal of biological chemistry High 30135210
2021 ERLIN2 links EVI/WLS (WNT secretory factor) to the ubiquitylation machinery within the ERAD pathway; EVI/WLS undergoes K11-, K48- and K63-linked ubiquitylation mediated by UBE2J2, UBE2K, and UBE2N, and this ubiquitylation is independent of E3 ligases HRD1 and GP78. Immunoblot-based RNAi screen, co-immunoprecipitation (ERLIN2–EVI/WLS), ubiquitin linkage-specific antibodies, E2/E3 knockdown Journal of cell science Medium 34406391
2023 The ERLIN2 heterozygous missense variant p.Val71Ala recruits the ubiquitin E3 ligase RNF213 to IP3R1, leading to IP3R1 degradation, reduced intracellular free calcium, ER stress-mediated apoptosis, and inhibition of the MAPK signaling pathway reducing cell proliferation. Patient-derived iPSC models, IP-mass spectrometry (identifying RNF213 interaction), IP3R1 degradation assay, calcium imaging, MAPK pathway analysis Human mutation Medium 40225166
2023 ERLIN2 heterozygous variant (V71A) causes altered ER morphology and increased XBP-1S mRNA (ER stress activation), and promotes axon growth when overexpressed in primary cortical neurons. HeLa cell immunofluorescence, RT-PCR (XBP-1 splicing), mouse primary cortical neuron overexpression with axon morphology quantification Annals of clinical and translational neurology Medium 37752894
2024 The erlin1/2 complex directly and selectively binds PI(3)P; disruption or deletion of the complex reduces cellular PI(3)P levels by ~50%, which correlates with decreased autophagic flux but no effect on the endocytic pathway; the reduction is not due to decreased VPS34 kinase activity, indicating erlin1/2 stabilizes PI(3)P pools to sustain autophagy. In vitro PI(3)P binding assay with recombinant erlins, PI(3)P quantification in cells with erlin KO/disruption, autophagic flux assay, VPS34 kinase activity measurement, pharmacological VPS34 inhibition Biochemical and biophysical research communications High 39018973
2025 ERLIN2 assists in cholesterol trafficking from the ER to the outer mitochondrial membrane via MAM by facilitating intermediate folding of the cholesterol transporter StAR; ERLIN2–StAR interactions are transient and increase progressively from ER to MAM; absence of ERLIN2 ablates mitochondrial cholesterol transport. Co-immunoprecipitation (ERLIN2–StAR at ER and MAM), ERLIN2 knockout/knockdown, mitochondrial cholesterol transport assay, StAR folding assay Molecular and cellular biology Medium 41251286
2025 Cryo-EM structures of the human erlin1/2 complex reveal a 26-mer (13 heterodimers of erlin1 and erlin2) ring-shaped assembly; the complex defines a nanodomain on the ER membrane that can cage cargo proteins (physically secluding them from binding partners) and interact with other cages to organize functional membrane microdomains of varying sizes. Single-particle cryo-EM structure determination under multiple detergent conditions, structural analysis of subunit interactions and conformational heterogeneity bioRxiv (preprint)preprint High bio_10.1101_2025.04.21.649849
2025 A second independent cryo-EM study confirms the erlin1/2 complex forms a 26-mer cage-like structure of alternating erlin1 and erlin2 subunits; the cage recruits proteins to both interior and exterior membrane regions, physically sequesters cargo, and individual cages further oligomerize to organize larger functional membrane microdomains on the ER. Single-particle cryo-EM under different detergent conditions, functional analysis of cargo sequestration and cage-cage interaction bioRxiv (preprint)preprint High bio_10.1101_2025.06.14.659634
2026 ERLIN2 regulates IP3R-mediated Ca2+ release and activates the CaMKII-MAPK-CREB signaling pathway, positively regulating CRY1/2 transcription and maintaining circadian rhythmicity in skeletal muscle cells; ERLIN2 knockdown or overexpression alters circadian amplitude, and ATP-induced IP3R-dependent Ca2+ transients that reshape circadian phase are blocked by IP3R, Ca2+, or CaMKII inhibition. C2C12 skeletal muscle cell knockdown and overexpression, circadian reporter assays, Ca2+ imaging, pharmacological inhibition of IP3R/CaMKII/MAPK, CREB phosphorylation assay, CRY1/2 transcription measurement FEBS letters Medium 41572931
2026 ERLIN2 undergoes N-glycosylation at asparagine 106 (N106); the E3 ubiquitin ligase MARCHF6 mediates ubiquitination and degradation of ERLIN2, with this effect enhanced when N106 glycosylation is inhibited (N106Q mutant); N-glycosylation at N106 enhances ERLIN2 interaction with Cyclin B1 (CCNB1) and promotes CCNB1 stabilization. Site-directed mutagenesis (N106Q), co-immunoprecipitation (ERLIN2–CCNB1), MARCHF6 knockdown/overexpression with ERLIN2 ubiquitination assay, N-glycosylation inhibition Molecular and cellular biochemistry Medium 42166002
2025 CLPTM1L interacts with ERLIN2 to cooperatively stabilize SREBP1 protein levels by inhibiting its ubiquitination; knockdown of ERLIN2 reduces SREBP1 levels and suppresses NPC cell proliferation and migration. Co-immunoprecipitation (CLPTM1L–ERLIN2), RNAi knockdown of ERLIN2 with SREBP1 ubiquitination and stability assays, cell proliferation/migration assays Cell death & disease Medium 40550808
2023 KCNN1 interacts with ERLIN2 and enhances ERLIN2-mediated Cyclin B1 stabilization and K63-linked ubiquitination; ERLIN2 knockdown partially reverses the KCNN1 overexpression-induced increase in Cyclin B1 stability, placing ERLIN2 downstream of KCNN1 in a KCNN1/ERLIN2/Cyclin B1 axis. Co-immunoprecipitation (KCNN1–ERLIN2), K63-ubiquitin-specific assay for Cyclin B1, epistasis by double knockdown/overexpression Carcinogenesis Medium 37831636

Source papers

Stage 0 corpus · 36 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER. Journal of cell science 198 16835267
2009 An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors. The Journal of biological chemistry 95 19240031
2007 SPFH2 mediates the endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors and other substrates in mammalian cells. The Journal of biological chemistry 90 17502376
2011 A nullimorphic ERLIN2 mutation defines a complicated hereditary spastic paraplegia locus (SPG18). Neurogenetics 68 21796390
2011 A frameshift mutation of ERLIN2 in recessive intellectual disability, motor dysfunction and multiple joint contractures. Human molecular genetics 62 21330303
2012 Loss of ERLIN2 function leads to juvenile primary lateral sclerosis. Annals of neurology 58 23109145
2012 ERLIN2 promotes breast cancer cell survival by modulating endoplasmic reticulum stress pathways. BMC cancer 33 22681620
2012 Endoplasmic reticulum factor ERLIN2 regulates cytosolic lipid content in cancer cells. The Biochemical journal 33 22690709
2018 MiR-410 Acts as a Tumor Suppressor in Estrogen Receptor-Positive Breast Cancer Cells by Directly Targeting ERLIN2 via the ERS Pathway. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 30 30016800
2018 A novel heterozygous variant in ERLIN2 causes autosomal dominant pure hereditary spastic paraplegia. European journal of neurology 29 29528531
2015 A novel ER-microtubule-binding protein, ERLIN2, stabilizes Cyclin B1 and regulates cell cycle progression. Cell discovery 28 27462423
2018 The erlin2 T65I mutation inhibits erlin1/2 complex-mediated inositol 1,4,5-trisphosphate receptor ubiquitination and phosphatidylinositol 3-phosphate binding. The Journal of biological chemistry 27 30135210
2012 A novel splice site mutation in ERLIN2 causes hereditary spastic paraplegia in a Saudi family. European journal of medical genetics 25 23085305
2009 SPFH1 and SPFH2 mediate the ubiquitination and degradation of inositol 1,4,5-trisphosphate receptors in muscarinic receptor-expressing HeLa cells. Biochimica et biophysica acta 24 19751772
2021 EVI/WLS function is regulated by ubiquitylation and is linked to ER-associated degradation by ERLIN2. Journal of cell science 19 34406391
2012 Erlin-2 is associated with active γ-secretase in brain and affects amyloid β-peptide production. Biochemical and biophysical research communications 17 22771797
2019 Spastic paraplegia due to recessive or dominant mutations in ERLIN2 can convert to ALS. Neurology. Genetics 16 32042907
2020 An autosomal dominant ERLIN2 mutation leads to a pure HSP phenotype distinct from the autosomal recessive ERLIN2 mutations (SPG18). Scientific reports 15 32094424
2020 Expansion of the genetic landscape of ERLIN2-related disorders. Annals of clinical and translational neurology 15 32147972
2020 SNHG17 drives malignant behaviors in astrocytoma by targeting miR-876-5p/ERLIN2 axis. BMC cancer 9 32883232
2020 Molecular and Immune Characteristics for Lung Adenocarcinoma Patients With ERLIN2 Overexpression. Frontiers in immunology 9 33424830
1999 Cloning and characterization of a novel gene (C8orf2), a human representative of a novel gene family with homology to C. elegans C42.C1.9. Cytogenetics and cell genetics 9 10449903
2021 More autosomal dominant SPG18 cases than recessive? The first AD-SPG18 pedigree in Chinese and literature review. Brain and behavior 8 34734492
2023 A novel autosomal dominant ERLIN2 variant activates endoplasmic reticulum stress in a Chinese HSP family. Annals of clinical and translational neurology 4 37752894
2023 KCNN1 promotes proliferation and metastasis of breast cancer via ERLIN2-mediated stabilization and K63-dependent ubiquitination of Cyclin B1. Carcinogenesis 3 37831636
2024 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 2 38607533
2024 The erlin1/erlin2 complex binds to and stabilizes phosphatidylinositol 3-phosphate and regulates autophagy. Biochemical and biophysical research communications 2 39018973
2025 Association of novel ERLIN2 gene variants with hereditary spastic paraplegia. Human genome variation 1 39762222
2025 CLPTM1L interacts with ERLIN2 to stabilize SREBP1 and drive tumorigenesis in nasopharyngeal carcinoma. Cell death & disease 1 40550808
2024 Hereditary spastic paraparesis type 18 (SPG18): new ERLIN2 variants in a series of Italian patients, shedding light upon genetic and phenotypic variability. Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology 1 38427163
2023 Novel ERLIN2 variant expands the phenotype of Spastic Paraplegia 18. Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology 1 38159148
2023 Disruption of Intracellular Calcium Homeostasis Leads to ERLIN2-Linked Hereditary Spastic Paraplegia in Patient-Derived Stem Cell Models. Human mutation 1 40225166
2009 A novel porcine gene--erlin2, differentially expressed in the liver tissues from Meishan and Large White pigs. Applied biochemistry and biotechnology 1 19421723
2026 ERLIN2-Ca2+-CREB signaling coordinates circadian timing via CRY1/CRY2 feedback. FEBS letters 0 41572931
2026 N-glycosylation of ERLIN2 promotes hepatocellular carcinoma progression by enhancing CCNB1 stability. Molecular and cellular biochemistry 0 42166002
2025 Cholesterol Transport from ER to Outer Mitochondria by ERLIN2 in Steroid Metabolism. Molecular and cellular biology 0 41251286

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