Affinage

ESYT2

Extended synaptotagmin-2 · UniProt A0FGR8

Length
921 aa
Mass
102.4 kDa
Annotated
2026-06-09
43 papers in source corpus 19 papers cited in narrative 19 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

ESYT2 (E-Syt2) is an ER-resident transmembrane protein that tethers the endoplasmic reticulum to the plasma membrane and acts as a lipid transfer and signaling platform at membrane contact sites (PMID:23791178, PMID:24847877). It is anchored to the ER by its transmembrane domain and engages the plasma membrane through its C-terminal C2 domains: the C2C domain serves as a PI(4,5)P2-dependent PM-targeting motif, while the C2A domain binds phospholipids in a Ca2+-dependent manner, with structural and single-molecule studies establishing a rigid V-shaped tandem-C2 architecture and quantifying its calcium-tuned membrane affinity (PMID:17360437, PMID:24373768, PMID:29083305). E-Syt2 forms heteromeric complexes with E-Syt1 and E-Syt3, and its dimeric SMP domain folds into a TULIP-superfamily hydrophobic channel that binds and transfers glycerophospholipids between apposed membranes (PMID:23791178, PMID:24847877). At ER-PM junctions it controls phosphoinositide homeostasis by positioning the lipid phosphatase Sac1 to limit PM PI(4)P, a coupling that is dynamically regulated by GPCR-driven PI(4,5)P2 depletion and by upstream control of PM PI(4,5)P2 through RASSF4-ARF6-PIP5K signaling (PMID:27044890, PMID:28600435). Through these lipid functions E-Syt2 shapes signaling at the PM: it lowers plasma membrane DAG to downmodulate T-cell receptor signaling, and a short isoform recruits STIM1 to support CRAC-channel-mediated store-operated Ca2+ entry in T cells (PMID:38177911, PMID:32879390). Beyond ER-PM contacts, E-Syt2 forms a complex with E-Syt1 and VAPB at lipid droplet-mitochondria-ER contacts to enable fatty acid oxidation, with its deletion causing lipotoxic stress and TCA-cycle metabolite depletion in cells and mice (PMID:40032835). Independently, E-Syt2 functions as an endocytic adaptor for activated FGFR1, interacting with the receptor through a TM-adjacent sequence and with Adaptin-2 and PAK1 to couple receptor endocytosis to actin dynamics and ERK signaling (PMID:20833364, PMID:23213466, PMID:25922075).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 2007 High

    Established the domain logic of E-Syt2 membrane engagement, showing how a multi-C2 protein could be targeted to the plasma membrane and respond to calcium.

    Evidence Recombinant Ca2+-dependent phospholipid binding assays plus domain-deletion localization of myc-tagged constructs

    PMID:17360437

    Open questions at the time
    • Did not place the protein at ER-PM contacts or define a cellular function
    • ER anchoring versus PM targeting roles not yet separated
  2. 2008 Medium

    Quantified the calcium responsiveness of the C2 region, showing Ca2+-triggered conformational change and multimerization in vitro.

    Evidence SAXS of the recombinant soluble multi-C2 region with quantitative Ca2+ binding (~100 µM)

    PMID:18977228

    Open questions at the time
    • Solution behavior not linked to membrane tethering in cells
    • Functional consequence of multimerization undefined
  3. 2010 High

    Revealed an unexpected role for E-Syt2 as an endocytic adaptor required for FGF receptor internalization and downstream ERK-driven mesoderm induction.

    Evidence Morpholino depletion in Xenopus, reciprocal Co-IP with FGFR and Adaptin-2, Ras/ERK epistasis and rescue

    PMID:20833364

    Open questions at the time
    • Relationship between endocytic adaptor role and later contact-site/lipid functions unresolved
    • Whether this role operates in mammalian somatic cells not addressed
  4. 2012 Medium

    Identified PAK1 as a direct C2C-domain partner, linking E-Syt2 to suppression of actin polymerization and to FGFR1-associated signaling complexes.

    Evidence Co-IP with C2C domain mapping, PAK1 activation and actin polymerization assays, FGFR1 complex analysis

    PMID:23213466

    Open questions at the time
    • Single lab without reciprocal in vivo validation
    • Integration with lipid-tethering activity not addressed
  5. 2013 High

    Defined E-Syt2 (with E-Syt3) as a constitutive PI(4,5)P2-dependent ER-PM tether that forms Ca2+-regulated heteromers with E-Syt1, establishing its core contact-site function.

    Evidence ER-PM contact imaging, PI(4,5)P2 manipulation, Ca2+ imaging, Co-IP, siRNA, STIM1/Orai1 epistasis

    PMID:23791178

    Open questions at the time
    • Mechanism of lipid handling at contacts not yet shown
    • Showed E-Syt contacts dispensable for SOCE, leaving downstream lipid roles open
  6. 2013 High

    Provided atomic detail of the tandem C2A-C2B module, showing a rigid Ca2+-independent architecture with Ca2+ binding confined to C2A.

    Evidence X-ray crystallography with and without Ca2+ and NMR Ca2+-binding analysis

    PMID:24373768

    Open questions at the time
    • Did not include the SMP domain or define lipid transfer
    • Membrane-bound conformation not resolved
  7. 2014 High

    Demonstrated that E-Syt2 is a lipid transfer protein, with a dimeric SMP β-barrel forming a hydrophobic channel that captures glycerophospholipids.

    Evidence 2.44 Å crystal structure of SMP-C2A-C2B and mass spectrometry of channel-bound lipids

    PMID:24847877

    Open questions at the time
    • Directionality and physiological lipid cargo in cells not established
    • Coupling of transfer to contact-site dynamics undefined
  8. 2014 Medium

    Mapped the topology and FGFR1-binding determinants of E-Syt2, showing TM-domain ER targeting, TM-adjacent homodimerization, and conformation-dependent FGFR1 recognition.

    Evidence Co-IP, systematic domain mutants, localization studies, kinase-dead receptor analysis

    PMID:25922075

    Open questions at the time
    • Single lab Co-IP-based interaction mapping
    • Functional consequence in mammalian FGFR signaling not quantified here
  9. 2016 High

    Connected E-Syt2 tethering to PM phosphoinositide homeostasis by showing it positions Sac1 to control PI(4)P, with junctions dynamically remodeled by GPCR and SOCE signaling.

    Evidence Live-cell imaging of E-Syt2/Sac1 colocalization, phosphoinositide biosensors, GPCR/SOCE manipulation, siRNA

    PMID:27044890

    Open questions at the time
    • Direct physical Sac1-E-Syt2 interaction not biochemically resolved
    • Quantitative contribution to total PM PI(4)P turnover unclear
  10. 2016 Medium

    Revealed splice-isoform-specific cellular functions, with short and long E-Syt2 variants differentially controlling actin distribution and endocytosis.

    Evidence Variant-specific siRNA, actin imaging and endocytosis assays in lung cancer cells

    PMID:27555542

    Open questions at the time
    • No molecular mechanism beyond variant specificity
    • Isoform-specific partners not identified here
  11. 2017 Medium

    Placed E-Syt2 tethering downstream of RASSF4-ARF6-PIP5K control of PM PI(4,5)P2, defining an upstream regulatory input.

    Evidence RASSF4 siRNA, ER-PM contact imaging, PI(4,5)P2 biosensor, ARF6 activity assay, Co-IP

    PMID:28600435

    Open questions at the time
    • Single lab
    • Direct versus indirect effect of RASSF4 on E-Syt2 not separated
  12. 2017 High

    Provided quantitative single-molecule force measurements of C2-domain membrane binding, mechanically validating bilayer- and Ca2+-tuned tethering.

    Evidence Optical-tweezers force spectroscopy across defined bilayers and Ca2+ conditions

    PMID:29083305

    Open questions at the time
    • Reconstituted system; in-cell forces not measured
    • Does not address lipid transfer flux
  13. 2017 Low

    Identified UBQLN1 as a stabilizer of ESYT2 protein levels, implicating proteostasis control of the tether.

    Evidence Co-IP with UBQLN1 domain mapping and Western blot stability assays

    PMID:28075048

    Open questions at the time
    • Single Co-IP with ESYT2 as one of several substrates, not independently confirmed
    • Physiological context of ESYT2 turnover undefined
  14. 2020 Medium

    Linked E-Syt2 to SNARE machinery and neuronal morphogenesis, showing it stabilizes Sec22b-Stx1 at ER-PM contacts and promotes axonal filopodia in a lipid-transfer- and tethering-dependent manner.

    Evidence Co-IP with Sec22b longin-domain mapping, E-Syt2 mutant analysis, neurite morphology quantification, neurotoxin epistasis

    PMID:32843578

    Open questions at the time
    • Single lab
    • Mechanistic coupling of lipid transfer to SNARE function not fully defined
  15. 2020 Medium

    Showed the short E-Syt2 isoform recruits STIM1 to ER-PM junctions to support CRAC channel activation, a tethering-independent, cell-type-specific role in T cells.

    Evidence CRISPR/siRNA knockdown, E-Syt2S-STIM1 Co-IP, SOCE Ca2+ imaging, Orai1-STIM1 clustering in Jurkat vs HeLa

    PMID:32879390

    Open questions at the time
    • Reconciliation with earlier finding that E-Syt contacts are dispensable for SOCE
    • Structural basis of E-Syt2S-STIM1 interaction unresolved
  16. 2021 Medium

    Used the C. elegans ortholog to show ESYT-2 acts antagonistically with junctophilin JPH-1 at neuronal contact sites in synaptic transmission.

    Evidence Colocalization and genetic double-mutant epistasis with aldicarb assay in C. elegans

    PMID:33871019

    Open questions at the time
    • Molecular basis of JPH-1 antagonism unknown
    • Conservation of this interaction in mammals not tested
  17. 2023 Medium

    Defined a signaling output of E-Syt2 lipid control, showing it lowers PM DAG to negatively regulate T-cell receptor signaling and effector function.

    Evidence E-Syt2/E-Syt1 knockdown/deletion in T cells, DAG biosensor imaging, cytokine/degranulation/cytotoxicity assays

    PMID:38177911

    Open questions at the time
    • Direct enzymatic link between E-Syt2 and DAG metabolism not established
    • Single lab
  18. 2025 High

    Extended E-Syt2 function to lipid droplet-mitochondria-ER contacts, showing it forms a complex with E-Syt1 and VAPB that supports fatty acid oxidation and protects against lipotoxic stress in vivo.

    Evidence BioID proximity proteomics, high-resolution imaging, ESYT2 KO in cells and mice, FAO assays, metabolomics and lipidomics

    PMID:40032835

    Open questions at the time
    • Whether lipid transfer activity directly drives FAO at these contacts not isolated
    • Mechanism of VAPB-dependent contact assembly undefined
  19. 2025 Medium

    Implicated E-Syt2 in chloride channel regulation, showing it remodels a junctional ANO1 signaling complex and reduces ANO1 Ca2+ affinity via PKA-dependent phosphorylation.

    Evidence Co-IP complex characterization, S221 phosphosite mutagenesis, ANO1 Ca2+ affinity measurements, phosphoinositide biosensors, knockdown/rescue

    PMID:40204782

    Open questions at the time
    • Single lab
    • Direct versus phosphoinositide-mediated contribution of E-Syt2 not fully separated

Open questions

Synthesis pass · forward-looking unresolved questions
  • How E-Syt2's distinct activities—lipid transfer, ER-PM tethering, endocytic adaptation, and isoform-specific signaling—are coordinately deployed across cell types and contact-site types remains unresolved.
  • Directionality and in vivo cargo selectivity of SMP-mediated lipid transfer unknown
  • No human disease link established in the corpus
  • Relative contributions of long versus short isoforms across tissues uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008289 lipid binding 3 GO:0060090 molecular adaptor activity 3 GO:0140104 molecular carrier activity 2
Localization
GO:0005783 endoplasmic reticulum 3 GO:0005886 plasma membrane 3 GO:0005739 mitochondrion 1 GO:0005811 lipid droplet 1
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-1430728 Metabolism 2 R-HSA-168256 Immune System 2 R-HSA-5653656 Vesicle-mediated transport 2
Partners
ESYT1ESYT3FGFR1PAK1RASSF4SEC22BSTIM1VAPB
Complex memberships
ANO1-IRBIT-E-Syt2-AC6-AKAP11-PKA complexE-Syt1/E-Syt2/E-Syt3 heteromerE-Syt2-PAK1-FGFR1 complexESYT2-ESYT1-VAPB lipid droplet-mitochondria-ER complex

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2007 E-Syt2 contains three C-terminal C2 domains; recombinant fragments including the C2A domain bind phospholipids in a Ca2+-dependent manner at micromolar free Ca2+ concentrations. The C2C domain of E-Syt2 functions as a targeting motif that localizes the protein to the plasma membrane independently of its transmembrane region. Recombinant protein biochemistry (Ca2+-dependent phospholipid binding assays), transfection of myc-tagged constructs with localization analysis, domain deletion/structure-function studies Proceedings of the National Academy of Sciences of the United States of America High 17360437
2008 The soluble multi-C2 domain region of E-Syt2 undergoes Ca2+-triggered structural rearrangements and reversible multimerization in vitro, with an apparent Ca2+-binding constant of ~100 µM, as determined by small-angle X-ray scattering (SAXS). Small-angle X-ray scattering (SAXS) of recombinant E-Syt2 protein; quantitative calcium binding analysis FEBS letters Medium 18977228
2010 E-Syt2 acts as an endocytic adaptor for clathrin-mediated endocytosis of the activated FGF receptor in Xenopus development; it interacts selectively with activated FGFR and with Adaptin-2, and is required upstream of Ras activation for ERK activation and mesoderm induction. Morpholino-based depletion in Xenopus embryos, co-immunoprecipitation with FGFR and Adaptin-2, epistasis with Ras/ERK pathway, rescue experiments, in vivo endocytosis assays Developmental cell High 20833364
2012 The C2C domain of E-Syt2 directly binds a site adjacent to the CRIB/GBD domain of PAK1; this interaction suppresses actin polymerization, inhibits PAK1 activation by Cdc42 and Rac, and E-Syt2–PAK1 complexes selectively associate with FGFR1 to cooperate in FGF signaling. Co-immunoprecipitation, domain mapping (C2C domain pulldown), functional PAK1 activation assays, actin polymerization assays, FGFR1 complex analysis Biology open Medium 23213466
2013 E-Syt2 and E-Syt3 tether the ER to the plasma membrane via C2 domain-dependent interactions requiring PI(4,5)P2; elevation of cytosolic Ca2+ is additionally required for E-Syt1-mediated tethering. The E-Syts form heteromeric complexes, conferring Ca2+ regulation to ER-PM contact formation. E-Syt-mediated contacts are not required for store-operated Ca2+ entry. Fluorescence microscopy (ER-PM contact site quantification), PI(4,5)P2 manipulation, Ca2+ imaging, co-immunoprecipitation (heteromeric complex), siRNA knockdown, STIM1/Orai1 epistasis Cell High 23791178
2013 Crystal structures of the tandem C2A-C2B domains of E-Syt2 reveal a rigid V-shaped architecture not substantially altered by Ca2+. The C2A domain binds up to four Ca2+ ions while the C2B domain does not bind Ca2+. NMR confirmed these Ca2+-binding properties. X-ray crystallography (structures in absence and presence of Ca2+), NMR spectroscopy for Ca2+-binding analysis Structure High 24373768
2014 The crystal structure of an E-Syt2 fragment (SMP domain plus C2A-C2B) at 2.44 Å resolution reveals a TULIP superfamily β-barrel SMP domain that dimerizes to form a ~90-Å hydrophobic channel. Mass spectrometry identified glycerophospholipids bound within this channel, demonstrating that E-Syt2 directly binds and likely transfers lipids via its SMP domain. X-ray crystallography (2.44 Å resolution crystal structure), mass spectrometry (lipid identification from SMP channel) Nature High 24847877
2014 ESyt2 is directed to the ER by its transmembrane domain. ESyt2 homodimerizes in vivo via a TM-adjacent sequence (not the SMP domain). ESyt2 (and ESyt3, but not ESyt1) selectively interacts with activated FGFR1 in vivo through a short TM-adjacent sequence; this interaction is independent of receptor autophosphorylation but dependent on receptor conformation (upper kinase lobe site revealed upon activation loop displacement). Co-immunoprecipitation, domain deletion/mutagenesis constructs, localization studies, kinase-dead mutant analysis The Journal of biological chemistry Medium 25922075
2016 At steady state, E-Syt2 positions Sac1 (an integral ER membrane lipid phosphatase) at ER-PM junctions, where Sac1 limits PM PI(4)P levels. Activation of GPCRs depleting PM PI(4,5)P2 disrupts E-Syt2-mediated ER-PM junctions, reducing Sac1 access to the PM and allowing PI(4)P and PI(4,5)P2 recovery. ER Ca2+ depletion and SOCE activation increase Sac1 at the PM via E-Syt2 contacts, depleting PM PI(4)P. Fluorescence microscopy (E-Syt2 and Sac1 colocalization at ER-PM junctions), GPCR stimulation/PI(4,5)P2 depletion experiments, SOCE activation, phosphoinositide biosensors, siRNA knockdown The Journal of cell biology High 27044890
2016 ESYT2-short variant inhibition causes cortical redistribution of actin in lung cancer cells, whereas inhibition of the long variant increases endocytosis, revealing isoform-specific roles for ESYT2 in cytoskeletal organization and endocytosis. siRNA knockdown of individual ESYT2 splice variants, actin distribution imaging, endocytosis assays in lung cancer cells Molecular oncology Medium 27555542
2017 Single-molecule optical tweezers measurements show that C2 domains of E-Syt2 resist membrane unbinding forces of 2–7 pN and have binding energies of 4–14 kBT per C2 domain. Regulation by bilayer composition and Ca2+ recapitulated known properties of E-Syt2 C2 domains. Single-molecule force spectroscopy (optical tweezers), defined lipid bilayer compositions, Ca2+ titration eLife High 29083305
2017 RASSF4 regulates E-Syt2- and E-Syt3-mediated ER-PM tethering by controlling PM PI(4,5)P2 levels through ARF6-dependent activation of PIP5Ks. Knockdown of RASSF4 reduces PI(4,5)P2, impairing E-Syt2/3 localization to ER-PM junctions. siRNA knockdown of RASSF4, ER-PM contact site imaging, PI(4,5)P2 biosensor, ARF6 activity assay, co-immunoprecipitation (RASSF4-ARF6) The Journal of cell biology Medium 28600435
2017 UBQLN1 interacts with ESYT2 through its STI chaperone-like domains (not the UBA or UBL domains) and stabilizes ESYT2 protein levels in a manner dependent on UBQLN1's UBA domain interaction with ubiquitin. Co-immunoprecipitation, domain deletion constructs of UBQLN1, Western blot for protein stability Journal of cellular biochemistry Low 28075048
2020 Sec22b interacts with E-Syt2 via the longin domain of Sec22b. This interaction stabilizes Sec22b-Stx1 association at ER-PM contacts. Overexpression of wild-type E-Syt2 (but not lipid-transfer-deficient or ER-attachment mutants) increases axonal filopodia formation and neurite ramification; this effect requires Stx1 cleavage sensitivity and the Sec22b longin domain. Co-immunoprecipitation (Sec22b-E-Syt2 interaction), domain mutant analysis, overexpression and silencing in neurons, neurite morphology quantification, clostridial neurotoxin epistasis Journal of cell science Medium 32843578
2020 The short isoform of E-Syt2 (E-Syt2S) is the predominant E-Syt2 isoform in T cells and directly interacts with STIM1, recruiting it to ER-PM junctions independently of ER-PM membrane tethering, thereby supporting CRAC channel (Orai1-STIM1) activation and store-operated Ca2+ entry in Jurkat T cells but not in HeLa cells. CRISPR/siRNA knockdown, co-immunoprecipitation (E-Syt2S–STIM1), Ca2+ imaging (SOCE measurement), Orai1-STIM1 clustering imaging, isoform-specific expression analysis Scientific reports Medium 32879390
2021 In C. elegans, ESYT-2 colocalizes with junctophilin JPH-1 at membrane contact sites in neurons. Genetic double-mutant analysis shows that jph-1 and esyt-2 null mutants display mutual suppression of aldicarb response, indicating that JPH-1 and ESYT-2 have antagonistic roles in neuromuscular synaptic transmission. Fluorescence localization studies, genetic epistasis (double-mutant analysis), aldicarb sensitivity assay in C. elegans Genetics Medium 33871019
2023 E-Syt2 reduces plasma membrane DAG levels in resting T cells, thereby downmodulating T-cell receptor signaling, cytotoxicity, degranulation, and cytokine production. Upon TCR stimulation, both E-Syt1 and E-Syt2 negatively control TCR signaling through DAG reduction at the PM. Knockdown/deletion of E-Syt2 (and E-Syt1) in T cells, DAG biosensor imaging, TCR signaling readouts (cytokine production, degranulation, cytotoxicity assays) EMBO reports Medium 38177911
2025 ESYT2 forms a multimeric complex with ESYT1 and VAPB at lipid droplet–mitochondria–ER contact sites. Deletion of ESYT2 limits lipid droplet-derived fatty acid oxidation, depletes TCA cycle metabolites, remodels the cellular lipidome, and induces lipotoxic stress; these findings were recapitulated in Esyt2-deficient mice. Proximity-dependent biotinylation (BioID), high-resolution imaging, ESYT2 deletion (cell lines and mice), fatty acid oxidation assays, metabolomics (TCA cycle metabolites), lipidomics Nature communications High 40032835
2025 E-Syt2 dissociates the ANO1-VAPA interaction at STIM1 ER-PM junctions and forms an ANO1-IRBIT-E-Syt2-AC6-AKAP11-PKA complex that phosphorylates ANO1 at S221, markedly reducing ANO1 Ca2+ affinity. These effects are primarily mediated by E-Syt2 reciprocally regulating junctional PI(4)P, PI(4,5)P2, and PtdSer levels. Co-immunoprecipitation (complex assembly), phosphorylation site mutagenesis (S221), Ca2+ affinity measurements for ANO1, phosphoinositide biosensors, knockdown and rescue experiments Nature communications Medium 40204782

Source papers

Stage 0 corpus · 43 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2013 PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins. Cell 481 23791178
2014 Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. Nature 258 24847877
2007 E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 domains. Proceedings of the National Academy of Sciences of the United States of America 156 17360437
2016 Dynamic formation of ER-PM junctions presents a lipid phosphatase to regulate phosphoinositides. The Journal of cell biology 80 27044890
2016 A large-scale analysis of alternative splicing reveals a key role of QKI in lung cancer. Molecular oncology 67 27555542
2017 RASSF4 controls SOCE and ER-PM junctions through regulation of PI(4,5)P2. The Journal of cell biology 59 28600435
2010 Extended-synaptotagmin-2 mediates FGF receptor endocytosis and ERK activation in vivo. Developmental cell 56 20833364
2016 Extended Synaptotagmin (ESyt) Triple Knock-Out Mice Are Viable and Fertile without Obvious Endoplasmic Reticulum Dysfunction. PloS one 52 27348751
2017 Single-molecule force spectroscopy of protein-membrane interactions. eLife 50 29083305
2017 The STI and UBA Domains of UBQLN1 Are Critical Determinants of Substrate Interaction and Proteostasis. Journal of cellular biochemistry 48 28075048
2025 Proximity proteomics reveals a mechanism of fatty acid transfer at lipid droplet-mitochondria- endoplasmic reticulum contact sites. Nature communications 35 40032835
2016 Loss of all 3 Extended Synaptotagmins does not affect normal mouse development, viability or fertility. Cell cycle (Georgetown, Tex.) 35 27399837
2013 Structure and Ca²⁺-binding properties of the tandem C₂ domains of E-Syt2. Structure (London, England : 1993) 35 24373768
2017 Systematic identification of cancer-related long noncoding RNAs and aberrant alternative splicing of quintuple-negative lung adenocarcinoma through RNA-Seq. Lung cancer (Amsterdam, Netherlands) 28 28577945
2012 Proteomic study of the mucin granulae in an intestinal goblet cell model. Journal of proteome research 27 22248381
2020 Role of the Sec22b-E-Syt complex in neurite growth and ramification. Journal of cell science 25 32843578
2018 Oxysterol-binding protein-related protein (ORP) 6 localizes to the ER and ER-plasma membrane contact sites and is involved in the turnover of PI4P in cerebellar granule neurons. Experimental cell research 25 30028970
2013 Combined deletion of two Condensin II system genes (NCAPG2 and MCPH1) in a case of severe microcephaly and mental deficiency. European journal of medical genetics 25 24013099
2022 The genetic architecture of phenotypic diversity in the Betta fish (Betta splendens). Science advances 24 36129976
2017 A novel microscopy-based assay identifies extended synaptotagmin-1 (ESYT1) as a positive regulator of anoctamin 1 traffic. Biochimica et biophysica acta. Molecular cell research 23 29154949
2014 Loss of Extended Synaptotagmins ESyt2 and ESyt3 does not affect mouse development or viability, but in vitro cell migration and survival under stress are affected. Cell cycle (Georgetown, Tex.) 21 25486202
2009 Candidate genes associated with malignant pheochromocytomas by genome-wide expression profiling. Annals of surgery 20 19661783
2024 Early-stage idiopathic Parkinson's disease is associated with reduced circular RNA expression. NPJ Parkinson's disease 19 38245550
2021 Chemoproteomic profiling reveals cellular targets of nitro-fatty acids. Redox biology 19 34509914
2017 An investigation of obesity susceptibility genes in Northern Han Chinese by targeted resequencing. Medicine 19 28207535
2012 The endocytic adapter E-Syt2 recruits the p21 GTPase activated kinase PAK1 to mediate actin dynamics and FGF signalling. Biology open 17 23213466
2021 Caenorhabditis elegans junctophilin has tissue-specific functions and regulates neurotransmission with extended-synaptotagmin. Genetics 15 33871019
2020 The short isoform of extended synaptotagmin-2 controls Ca2+ dynamics in T cells via interaction with STIM1. Scientific reports 14 32879390
2015 Extended Synaptotagmin Interaction with the Fibroblast Growth Factor Receptor Depends on Receptor Conformation, Not Catalytic Activity. The Journal of biological chemistry 12 25922075
2022 Enforced tethering elongates the cortical endoplasmic reticulum and limits store-operated Ca2+ entry. Journal of cell science 10 35191477
2007 Two independent chromosomal rearrangements, a very small (550 kb) duplication of the 7q subtelomeric region and an atypical 17q11.2 (NF1) microdeletion, in a girl with neurofibromatosis. Cytogenetic and genome research 8 18160797
2008 Structural characterization of soluble E-Syt2. FEBS letters 7 18977228
2014 Apical localization of inositol 1,4,5-trisphosphate receptors is independent of extended synaptotagmins in hepatocytes. PloS one 6 25437447
2025 Multiple cAMP/PKA complexes at the STIM1 ER/PM junction specified by E-Syt1 and E-Syt2 reciprocally gates ANO1 (TMEM16A) via Ca2. Nature communications 5 40204782
2024 The splicing factor QKI inhibits metastasis by modulating alternative splicing of E-Syt2 in papillary thyroid carcinoma. Cancer letters 5 39306227
2018 Membrane proteome characterization of periodontal ligament cell sets from deciduous and permanent teeth. Journal of periodontology 5 30499115
2023 Extended-Synaptotagmin-1 and -2 control T cell signaling and function. EMBO reports 4 38177911
2020 Data independent acquisition-mass spectrometry (DIA-MS)-based comprehensive profiling of bone metastatic cancers revealed molecular fingerprints to assist clinical classifications for bone metastasis of unknown primary (BMUP). Translational cancer research 3 35117599
2009 Expression and purification of soluble E-Syt2: low protein stability impedes tag removal. Journal of chromatography. B, Analytical technologies in the biomedical and life sciences 2 19398219
2024 Extended Synaptotagmins 1 and 2 Are Required for Store-Operated Calcium Entry, Cell Migration and Viability in Breast Cancer Cells. Cancers 1 39061158
2026 Quantitative FRET FLIM imaging reveals multiple interactions between proteins of the ESYT, ORP and VAP families at the endoplasmic reticulum membrane. The Journal of biological chemistry 0 42134546
2025 Genome-wide association for sarcoidosis identifies novel risk loci and genetic heritability in African and European ancestries: a meta-analysis from the Finngen, Million Veteran Program, UK Biobank, and Biobank Japan datasets. Orphanet journal of rare diseases 0 41466414
2022 Single-Molecule Optical Tweezers Study of Protein-Membrane Interactions. Methods in molecular biology (Clifton, N.J.) 0 35819776

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