Affinage

SEC22B

Vesicle-trafficking protein SEC22b · UniProt O75396

Length
215 aa
Mass
24.7 kDa
Annotated
2026-06-10
30 papers in source corpus 23 papers cited in narrative 23 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SEC22B is an R-SNARE of the ER/ERGIC that mediates anterograde ER-to-Golgi membrane transport and, through non-fusogenic SNARE pairings, participates in membrane contact-site biology, unconventional secretion, and immune membrane traffic (PMID:9950687, PMID:22153078). Its N-terminal longin domain adopts a profilin/GAF-like α/β fold structurally distinct from syntaxin 1A and dispensable for SNARE assembly kinetics in vitro (PMID:11309394). In canonical ER fusion, SEC22B binding to the Qa-SNARE syntaxin 18 increases α-helicity in both SNARE motifs to nucleate sequential recruitment of the Qb/Qc-SNAREs BNIP1 and p31/Use1 (PMID:17979832), and loss of SEC22B-dependent ER-to-Golgi transport disorganizes the Golgi, dilates the rough ER, and impairs VWF processing and secretion (PMID:32336681). Beyond classical fusion, the longin domain pairs SEC22B with plasma-membrane syntaxins (Stx1, Stx4) at ER-PM contact sites, stabilized by extended synaptotagmins, to drive neurite outgrowth (PMID:32843578) and to support unconventional secretion of cytosolic cargo loaded into SEC22B+ vesicles that tether to the PM via SNAP23-containing Q-SNARE complexes (PMID:36044553). In phagocytes, SEC22B pairs with phagosomal syntaxin 4 to deliver ER components to maturing phagosomes, sustain MHC class I cross-presentation, and tether ER-phagosome contact sites independently of STIM1; this tethering recruits the lipid-exchange protein ORP8 to set phagosomal PI(4)P, PS and PI(3)P content and restrain phagolysosome fusion and antigen degradation (PMID:22153078, PMID:37794132). SEC22B is also required for megakaryocyte α-granule biogenesis through its interaction with NBEAL2 (PMID:32384141) and for plasma cell maintenance and efficient antibody secretion (PMID:36595686). Intracellular Legionella exploits SEC22B by recruiting ER-derived vesicles to the Legionella-containing vacuole and driving non-canonical SEC22B pairing with plasma-membrane syntaxins; the bacterial effectors Lug15 and SdeA ubiquitinate SEC22B—SdeA installing phosphoribosyl-ubiquitin at serine 137 followed by canonical polyubiquitination—to promote these non-canonical complexes (PMID:15117975, PMID:20163564, PMID:37882795, PMID:41669755). The same residue is targeted physiologically: glucagon signaling phosphorylates SEC22B at S137 in hepatocytes to control glycogen, lipid, and amino acid metabolism (PMID:39333498).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 1999 High

    Established SEC22B as a functional component of early secretory traffic by showing it acts at the pre-Golgi intermediate compartment before the docking/fusion step of ER-to-Golgi transport.

    Evidence Immunofluorescence localization and antibody-inhibited semi-intact cell ER-Golgi transport reconstitution

    PMID:9950687

    Open questions at the time
    • Did not define the cognate Q-SNARE partners
    • Mechanism of vesicle docking versus fusion not resolved
  2. 2001 High

    Resolved the architecture of the SEC22B N-terminal domain, revealing a longin (profilin/GAF-like) fold that is structurally distinct from syntaxin 1A and does not govern SNARE assembly rate, reframing the domain's role away from kinetic regulation of fusion.

    Evidence X-ray crystallography at 2.4 Å plus in vitro SNARE assembly kinetics

    PMID:11309394

    Open questions at the time
    • Functional role of the longin fold left undefined
    • No partner identified for the domain at this stage
  3. 2008 Medium

    Defined the molecular logic of canonical ER SNARE assembly, showing SEC22B binding to syntaxin 18 induces α-helicity that creates high-affinity sites for BNIP1 and p31/Use1.

    Evidence Pulldown assays and CD spectroscopy of SNARE motif α-helicity changes

    PMID:17979832

    Open questions at the time
    • In vitro biophysics not validated by reconstituted fusion
    • Single-lab biophysical analysis
  4. 2009 Medium

    Showed SEC22B abundance negatively tunes phagocytosis through its R-SNARE motif, implicating it in regulating Q-SNARE availability in phagocytes.

    Evidence Overexpression, shRNA knockdown, and domain mapping with phagocytosis assays in macrophages

    PMID:19710423

    Open questions at the time
    • Titration model of free syntaxin 18/D12 not directly demonstrated
    • Single cell-line context
  5. 2011 High

    Connected SEC22B to immune membrane traffic by showing it pairs with phagosomal syntaxin 4 to deliver ER components to phagosomes and enable MHC class I cross-presentation.

    Evidence siRNA knockdown, Co-IP of SEC22B-syntaxin 4, phagosome maturation and cross-presentation assays in dendritic cells

    PMID:22153078

    Open questions at the time
    • Whether SEC22B mediates fusion versus non-fusogenic tethering at phagosomes unresolved here
    • Did not address contact-site lipid transfer
  6. 2017 Medium

    Tested the genetic requirement for SEC22B in cross-presentation in vivo, yielding conflicting conclusions on whether SEC22B is essential for DC cross-priming.

    Evidence Two independent DC-specific conditional knockout mouse lines with ex vivo/in vivo cross-presentation assays; one used shRNA-in-KO controls

    PMID:28658614 PMID:28663435

    Open questions at the time
    • The two conditional KO studies reach opposite conclusions
    • shRNA off-target effects confound earlier knockdown data
  7. 2020 High

    Extended SEC22B function beyond bulk traffic, establishing it as a longin-domain-mediated organizer at ER-PM contacts (with E-Syts and Stx1 for neurite growth) and as an essential factor for megakaryocyte α-granule biogenesis via NBEAL2.

    Evidence Co-IP with domain and disease-variant mapping, CRISPR knockout, and neurite/α-granule morphology assays

    PMID:32384141 PMID:32843578

    Open questions at the time
    • Whether the NBEAL2 and E-Syt pathways intersect mechanistically is unknown
    • Stoichiometry of non-fusogenic SEC22B-Stx1 complexes not defined
  8. 2021 Medium

    Linked SEC22B-dependent anterograde transport to specialized secretory organelle biology (Weibel-Palade body morphology and VWF processing) and broadened its immune signaling role to NO/cytokine production and NF-κB shuttling.

    Evidence shRNA knockdown with EM, VWF secretion assays in endothelial cells, and siRNA with NO/cytokine and NF-κB translocation readouts in dendritic cells

    PMID:32336681 PMID:34580108

    Open questions at the time
    • NF-κB shuttling link is correlative
    • Direct SNARE partners at WPBs not mapped
  9. 2022 Medium

    Identified SEC22B as a regulator of autophagosome retrograde transport and as a mediator of unconventional cytosolic protein secretion through SEC22B+ vesicles tethering to the PM at ER-PM contacts.

    Evidence Knockdown/overexpression with Atg7 epistasis in an MCAO/R model; Co-IP, fractionation, proximity ligation and cargo-E-Syt1 inhibition in liver cancer cells

    PMID:35654605 PMID:36044553

    Open questions at the time
    • Opposing SEC22B/Ykt6 regulation mechanism not biochemically defined
    • Cargo selection into SEC22B+ vesicles unresolved
  10. 2023 High

    Defined the mechanistic basis of SEC22B at ER-phagosome contacts as a tether that recruits ORP8 to set phagosomal phospholipid composition, and established non-redundant requirements in plasma cell maintenance and antibody secretion.

    Evidence siRNA, Co-IP with ORP8, MAPPER artificial-tether and P33 MCS-disrupting mutant rescue, lipid profiling and calcium imaging; conditional KO mice with ELISA and organelle morphology

    PMID:36595686 PMID:37794132

    Open questions at the time
    • How tethering is coordinated with SNARE pairing at the same membrane is unclear
    • Transcriptional identity link in plasma cells is correlative
  11. 2023 Medium

    Revealed that Legionella effectors hijack SEC22B by ubiquitinating it (via the E3 ligase Lug15) to drive recruitment to the LCV and non-canonical pairing with plasma-membrane syntaxin 3.

    Evidence In vitro ubiquitination, Co-IP, and intracellular bacterial growth assays

    PMID:37882795

    Open questions at the time
    • Ubiquitination site not defined in this study
    • Host enzymatic background not excluded
  12. 2024 Medium

    Identified SEC22B serine 137 as a physiological glucagon-regulated phosphosite controlling hepatic glycogen, lipid, and amino acid metabolism, expanding SEC22B's role into metabolic signaling.

    Evidence Time-resolved liver phosphoproteomics, hepatocyte-specific KO/overexpression mice, and Co-IP with phospho-site variants

    PMID:39333498

    Open questions at the time
    • Phospho-dependent binding partners not fully resolved
    • Link between SNARE/trafficking activity and metabolic output not mechanistically closed
  13. 2025 Medium

    Resolved the chemistry of bacterial SEC22B ubiquitination, showing SdeA installs phosphoribosyl-ubiquitin at S137 followed by canonical polyubiquitination, with the deubiquitinase LotB reversing the syntaxin 3 pairing.

    Evidence In vitro ubiquitination, S137 mutagenesis, Co-IP, and LotB deubiquitinase assay

    PMID:41669755

    Open questions at the time
    • Temporal interplay of Lug15 and SdeA modifications not defined
    • Single-lab in vitro reconstitution
  14. 2025 Low

    Preprint-stage evidence extends SEC22B to ClC-5 secretory trafficking, secretory autophagy of UBB+1, and NRZ-coupled axonal ER-to-PM delivery of locally translated proteins.

    Evidence Co-IP and localization (ClC-5), siRNA secretion/fusion assays (UBB+1), live imaging and dominant-negative constructs (axonal NRZ-SEC22B)

    PMID:bio_10.1101_2024.12.31.630908 PMID:bio_10.1101_2025.09.09.674816 PMID:bio_10.1101_2025.11.03.686312

    Open questions at the time
    • All three are preprints lacking in vitro reconstitution
    • Single-lab observations not independently confirmed

Open questions

Synthesis pass · forward-looking unresolved questions
  • How SEC22B switches between fusogenic ER-to-Golgi transport and non-fusogenic tethering at ER-PM/ER-phagosome contacts, and how S137 modification states integrate metabolic, infection, and trafficking outputs, remain unresolved.
  • No unified model linking longin-domain tethering to SNARE-zippering decisions
  • Regulatory hierarchy of S137 phosphorylation versus ubiquitination unknown
  • Contradictory cross-presentation KO data still unreconciled

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 3 GO:0060090 molecular adaptor activity 2 GO:0008289 lipid binding 1
Localization
GO:0005783 endoplasmic reticulum 3 GO:0005886 plasma membrane 2 GO:0031410 cytoplasmic vesicle 2
Pathway
R-HSA-168256 Immune System 2 R-HSA-5653656 Vesicle-mediated transport 2 R-HSA-9609507 Protein localization 2 R-HSA-9612973 Autophagy 1
Partners
BNIP1NBEAL2ORP8SNAP23STX1STX18STX4USE1
Complex memberships
NRZ tethering complexSEC22B-syntaxin18-BNIP1-Use1 ER SNARE complex

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 Crystal structure of the 130-amino acid N-terminal (longin) domain of mouse Sec22b was solved at 2.4 Å resolution, revealing a mixed α/β fold resembling a circular permutation of profilin and GAF/PAS modules. This domain is structurally distinct from syntaxin 1A's N-terminal domain and, unlike syntaxin 1A, does not affect the rate of SNARE assembly in vitro. X-ray crystallography (2.4 Å), in vitro SNARE assembly kinetics assay The Journal of biological chemistry High 11309394
1999 Endogenous Sec22b/ERS-24 localizes to the pre-Golgi intermediate compartment (IC), and antibodies against Sec22b inhibit ER-to-Golgi transport of VSVG prior to the EGTA-sensitive docking/fusion step, causing VSVG accumulation in pre-Golgi vesicular intermediates. Immunofluorescence co-labeling, semi-intact cell ER-Golgi transport reconstitution assay with inhibitory antibodies, EGTA block-release Molecular biology of the cell High 9950687
2004 Sec22b localizes on ER-derived vesicles that are recruited to the Legionella-containing vacuole (LCV); Sec22b is delivered to the LCV membrane and is functionally required for biogenesis of the replicative organelle supporting Legionella intracellular growth. Rab1 recruits ER-derived vesicles to the LCV upstream of Sec22b-dependent fusion. Immunofluorescence/electron microscopy localization, genetic inhibition (dominant-negative constructs), intracellular growth assays The Journal of experimental medicine High 15117975
2008 Sec22b (R-SNARE) associates with ER-localized syntaxin 18 (Qa-SNARE), and this binary interaction induces increased α-helicity in both SNARE motifs, creating high-affinity binding sites for BNIP1 (Qb) and p31/Use1 (Qc), thereby driving sequential Q-SNARE assembly. This R-SNARE-dependent Q-SNARE assembly mechanism is distinct from that of non-ER SNAREs. Pulldown assays, CD spectroscopy measuring α-helicity changes upon SNARE motif association The Biochemical journal Medium 17979832
2009 Overexpression of Sec22b in J774 macrophages nearly abolishes phagocytosis without affecting Fc receptor surface expression, whereas suppression of endogenous Sec22b increases phagocytic capacity. Domain analysis shows the R-SNARE motif (responsible for SNARE complex formation with syntaxin 18 and/or D12) mediates this inhibition, identifying Sec22b as a negative regulator of phagocytosis likely by titrating free syntaxin 18/D12. Stable overexpression, shRNA knockdown, domain deletion/mutagenesis analysis, phagocytosis assay, flow cytometry Molecular biology of the cell Medium 19710423
2010 During virulent L. pneumophila infection, Sec22b (ER v-SNARE) undergoes non-canonical pairing with plasma membrane syntaxins (Stx2, Stx3, Stx4) and SNAP23 on the LCV. Depletion of plasma membrane syntaxins delays calnexin acquisition and retains Rab1 on phagosomes. Addition of α-SNAP and NSF dissociates these non-canonical SNARE complexes, demonstrating they are functional. RNAi depletion, co-immunoprecipitation, NSF/α-SNAP disassembly assay, immunofluorescence Traffic (Copenhagen, Denmark) High 20163564
2011 Sec22b localizes to the ERGIC and pairs with plasma membrane SNARE syntaxin 4 present on phagosomes. Depletion of Sec22b in dendritic cells inhibits recruitment of ER-resident proteins to phagosomes (and to T. gondii-containing vacuoles), impairs antigen export to the cytosol, accelerates lysosomal recruitment, and blocks MHC class I cross-presentation after phagocytosis or endocytosis of antigen. siRNA knockdown, immunofluorescence, co-immunoprecipitation (Sec22b–syntaxin 4 pairing), antigen cross-presentation assay, phagosome maturation assay Cell High 22153078
2017 DC-specific conditional knockout of Sec22b in mice impairs cross-presentation ex vivo and cross-priming of CD8+ T cells in vivo, and abolishes antitumor immune responses and response to anti-PD-1 therapy, supporting Sec22b-dependent ER-phagosome traffic as required for cross-presentation. Conditional Cre-lox DC-specific knockout mice, ex vivo cross-presentation assay, in vivo tumor challenge, anti-PD-1 treatment The Journal of experimental medicine Medium 28663435
2017 A separate DC-specific Sec22b knockout mouse (CD11c-Cre Sec22b fl/fl) shows that SEC22B-deficient DCs can efficiently cross-present antigen both in vivo and in vitro. shRNA-mediated Sec22b silencing reduces cross-presentation even in SEC22B-knockout BMDCs, indicating the shRNA effect is due to off-target activity rather than Sec22b loss. Conditional Cre-lox DC-specific knockout mice, in vitro/in vivo cross-presentation assays, shRNA in KO cells, RNA-seq of shRNA-treated KO BMDCs Cell reports Medium 28658614
2020 SEC22B interacts with NBEAL2 (gray platelet syndrome protein) via a region spanning NBEAL2 amino acids 1798–1903; GPS-associated missense variants E1833K and R1839C in NBEAL2 abolish this interaction. NBEAL2 can simultaneously bind SEC22B and P-selectin. CRISPR/Cas9 knockout of SEC22B in imMKCL cells decreases NBEAL2 protein and blocks α-granule biogenesis, demonstrating SEC22B is required for megakaryocyte α-granule production. Co-immunoprecipitation (tagged and endogenous proteins), CRISPR/Cas9 knockout, immunofluorescence microscopy, α-granule content assays Blood High 32384141
2020 Sec22b interacts with members of the extended synaptotagmin (E-Syt) family via the longin domain of Sec22b, stabilizing Sec22b–syntaxin 1 (Stx1) non-fusogenic SNARE complexes at ER-PM contacts. Overexpression of wild-type E-Syt2 (but not lipid-transfer-deficient or ER-anchoring-deficient mutants) increases axonal filopodia formation and neurite ramification; this effect is blocked by clostridial neurotoxin cleaving Stx1, longin domain expression, or a Sec22b mutant with an extended SNARE-TM linker. Co-immunoprecipitation, overexpression/dominant-negative constructs, neurite morphology assay, clostridial neurotoxin inhibition Journal of cell science Medium 32843578
2021 Sec22b depletion in endothelial cells causes loss of elongated Weibel-Palade body morphology, disintegration of Golgi and dilation of rough ER, reduced proteolytic processing of VWF, accumulation of VWF in dilated rER, and reduced VWF secretion, demonstrating that Sec22b-containing SNARE complexes governing ER-to-Golgi anterograde transport determine WPB length and VWF hemostatic activity. shRNA-mediated knockdown, immunofluorescence, electron microscopy, VWF secretion assay Haematologica Medium 32336681
2021 Sec22b co-localizes with inducible NO synthase (iNOS) at ERGIC/Golgi compartments and phagosomes. siRNA silencing of Sec22b in bone marrow-derived dendritic cells abrogates NO and cytokine production at both protein and mRNA levels and reduces nuclear translocation of NF-κB. Sec22b was found to co-occur with NF-κB in both cytoplasm and nucleus, implicating Sec22b in NF-κB shuttling. Immunofluorescence co-localization, siRNA knockdown, NO/cytokine measurement, NF-κB nuclear translocation assay, pharmacological secretory pathway blockade Journal of immunology Medium 34580108
2022 Sec22b and Ykt6 act as opposing regulators of autophagosome axonal retrograde transport in neurons. Ischemia-reperfusion increases Sec22b and decreases Ykt6 in neurons. Sec22b knockdown and Ykt6 overexpression rescue axonal autophagosome retrograde transport, restore autophagic flux, and reduce infarct size in a murine MCAO/R model in an autophagy-dependent manner. Knockdown/overexpression in primary neurons and in vivo murine MCAO/R model, live autophagosome tracking, autophagic flux assays, Atg7 conditional KO epistasis The Journal of neuroscience Medium 35654605
2022 In liver cancer cells, cytosolic proteins associate with E-Syt1 on the ER, then localize inside SEC22B+ vesicles. SEC22B on these vesicles tethers to the plasma membrane via Q-SNAREs (SNAP23, SNX3, SNX4) for secretion of cytosolic cargo, identifying SEC22B as a mediator of unconventional cytosolic protein secretion at ER-PM contact sites. Co-immunoprecipitation, subcellular fractionation, immunofluorescence, proximity ligation, inhibition of PKCδ–E-Syt1 interaction Proceedings of the National Academy of Sciences of the United States of America Medium 36044553
2023 Sec22b tethers ER-phagosome membrane contact sites (MCS) independently of STIM1. Sec22b knockdown increases phagosomal calcium signaling, accelerates phagolysosome fusion and antigen degradation, and alters phagosomal phospholipids (PI(3)P, PS, PI(4)P). Sec22b co-precipitates with the PS/PI(4)P exchange protein ORP8; wild-type but not catalytic-mutant ORP8 rescues phagosomal PI(4)P levels and reduces antigen degradation. The MCS-disrupting Sec22b-P33 mutant fails to rescue, identifying tethering as the mechanistic basis. siRNA knockdown, co-immunoprecipitation (Sec22b–ORP8), artificial tether (MAPPER) rescue, Sec22b-P33 MCS-disrupting mutant, phagosomal lipid quantification, calcium imaging, phagolysosome fusion assay Communications biology High 37794132
2023 The L. pneumophila effector Lug15 is a novel E3 ubiquitin ligase that ubiquitinates host Sec22b, mediates Sec22b recruitment to the LCV, and promotes non-canonical SNARE pairing of Sec22b with plasma membrane syntaxin 3. In vitro ubiquitination assay, co-immunoprecipitation, intracellular bacterial growth assay mBio Medium 37882795
2023 Sec22b is a critical non-redundant regulator of plasma cell maintenance: Sec22b-deficient mice show near-absence of plasma cells and dramatically reduced serum antibody titers. Mechanistically, Sec22b contributes to efficient antibody secretion and regulates transcriptional identity of plasma cells as well as morphology of the ER and mitochondria. Conditional knockout mice, flow cytometry, ELISA for antibody titers, immunofluorescence of organelle morphology, transcriptional profiling Proceedings of the National Academy of Sciences of the United States of America Medium 36595686
2024 Glucagon signaling phosphorylates SEC22B at serine 137 in the liver; hepatocyte-specific loss- and gain-of-function experiments show SEC22B is a key regulator of hepatic glycogen, lipid, and amino acid metabolism. SEC22B-S137 phosphorylation affects several protein binding partners and mediates glucagon's metabolic actions. In situ time-resolved liver phosphoproteomics, hepatocyte-specific KO and overexpression mouse models, co-immunoprecipitation of SEC22B binding partners with phospho-site variants Nature communications Medium 39333498
2025 The L. pneumophila effector SdeA catalyzes conjugation of phosphoribosyl-linked ubiquitin specifically to serine 137 of Sec22b; subsequently the canonical ubiquitin system adds polyubiquitin chains. This multimodal ubiquitination of Sec22b facilitates non-canonical SNARE pairing (Sec22b with Stx3) during early infection. The Legionella deubiquitinase LotB cleaves the polyubiquitin chains from Sec22b, causing Sec22b dissociation from syntaxin 3. In vitro ubiquitination assay, site-directed mutagenesis (Sec22b-S137), co-immunoprecipitation, deubiquitinase assay (LotB) iScience Medium 41669755
2025 SEC22B specifically interacts with wild-type ClC-5 chloride/proton antiporter but not with pathogenic ClC-5 mutants in renal proximal tubule cells. SEC22B deletion impairs ClC-5 trafficking, causing its retention at the Golgi and endosomes, identifying SEC22B as a trafficking factor for ClC-5 in the secretory pathway. Interactome analysis (Co-IP), CRISPR/Cas9 or siRNA knockdown, immunofluorescence of ClC-5 localization bioRxivpreprint Low bio_10.1101_2025.11.03.686312
2025 SEC22B (R-SNARE), together with Q-SNAREs STX4 and SNAP23, mediates fusion of UBB+1-containing autophagosomes with the plasma membrane during secretory autophagy. Disruption of SEC22B impairs autophagosome-PM fusion and reduces UBB+1 secretion without affecting its intracellular turnover. siRNA knockdown, secretion assay, autophagosome-PM fusion assay bioRxivpreprint Low bio_10.1101_2024.12.31.630908
2025 In axons, the NRZ–SEC22B tethering complex links axonal ER exit (ERES-dependent, Golgi-independent) to plasma membrane delivery of locally translated transmembrane proteins, dependent on ER-PM contacts. This coupling supports axon growth and bouton assembly. Live imaging in neurons, overexpression/dominant-negative constructs, ERES marker colocalization, axon growth and bouton assays bioRxivpreprint Low bio_10.1101_2025.09.09.674816

Source papers

Stage 0 corpus · 30 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 Sec22b regulates phagosomal maturation and antigen crosspresentation by dendritic cells. Cell 251 22153078
2004 Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle. The Journal of experimental medicine 245 15117975
2017 Critical role for Sec22b-dependent antigen cross-presentation in antitumor immunity. The Journal of experimental medicine 103 28663435
2010 Legionella pneumophila promotes functional interactions between plasma membrane syntaxins and Sec22b. Traffic (Copenhagen, Denmark) 86 20163564
2001 A novel snare N-terminal domain revealed by the crystal structure of Sec22b. The Journal of biological chemistry 69 11309394
1999 Morphological and functional association of Sec22b/ERS-24 with the pre-Golgi intermediate compartment. Molecular biology of the cell 55 9950687
2017 A Critical Analysis of the Role of SNARE Protein SEC22B in Antigen Cross-Presentation. Cell reports 37 28658614
2009 Sec22b is a negative regulator of phagocytosis in macrophages. Molecular biology of the cell 37 19710423
2020 The function of SEC22B and its role in human diseases. Cytoskeleton (Hoboken, N.J.) 27 32748571
2008 Sec22b-dependent assembly of endoplasmic reticulum Q-SNARE proteins. The Biochemical journal 27 17979832
1998 Hsec22c: a homolog of yeast Sec22p and mammalian rsec22a and msec22b/ERS-24. Biochemical and biophysical research communications 26 9501016
2020 The endoplasmic reticulum protein SEC22B interacts with NBEAL2 and is required for megakaryocyte α-granule biogenesis. Blood 25 32384141
2020 Role of the Sec22b-E-Syt complex in neurite growth and ramification. Journal of cell science 25 32843578
2017 MHC Class I Cross-Presentation: Stage Lights on Sec22b. Trends in immunology 17 28743621
2017 MHC I presentation of Toxoplasma gondii immunodominant antigen does not require Sec22b and is regulated by antigen orientation at the vacuole membrane. European journal of immunology 16 28508576
2021 Sec22b determines Weibel-Palade body length by controlling anterograde ER-Golgi transport. Haematologica 15 32336681
2023 Sec22b is a critical and nonredundant regulator of plasma cell maintenance. Proceedings of the National Academy of Sciences of the United States of America 14 36595686
2022 Unbalanced Regulation of Sec22b and Ykt6 Blocks Autophagosome Axonal Retrograde Flux in Neuronal Ischemia-Reperfusion Injury. The Journal of neuroscience : the official journal of the Society for Neuroscience 14 35654605
2022 Extended-synaptotagmin 1 engages in unconventional protein secretion mediated via SEC22B+ vesicle pathway in liver cancer. Proceedings of the National Academy of Sciences of the United States of America 13 36044553
2023 Sec22b regulates phagosome maturation by promoting ORP8-mediated lipid exchange at endoplasmic reticulum-phagosome contact sites. Communications biology 9 37794132
2023 Ubiquitination of Sec22b by a novel Legionella pneumophila ubiquitin E3 ligase. mBio 9 37882795
2019 SNARE protein SEC22B regulates early embryonic development. Scientific reports 9 31391476
2021 Sec22b Regulates Inflammatory Responses by Controlling the Nuclear Translocation of NF-κB and the Secretion of Inflammatory Mediators. Journal of immunology (Baltimore, Md. : 1950) 7 34580108
2024 Phosphoproteomics-directed manipulation reveals SEC22B as a hepatocellular signaling node governing metabolic actions of glucagon. Nature communications 5 39333498
2023 SEC22B inhibition attenuates colorectal cancer aggressiveness and autophagic flux under unfavorable environment. Biochemical and biophysical research communications 4 37148741
2023 Sec22b and Stx4 Depletion Has No Major Effect on Cross-Presentation of PLGA Microsphere-Encapsulated Antigen and a Synthetic Long Peptide In Vitro. Journal of immunology (Baltimore, Md. : 1950) 4 37638825
2020 Upregulation of Sec22b plays a neuroprotective role in a rat model of traumatic brain injury via inducing protective autophagy. Brain research bulletin 3 33186631
2023 Sec22b-dependent antigen cross-presentation is a significant contributor of T cell priming during infection with the parasite Trypanosoma cruzi. Frontiers in cell and developmental biology 1 36936692
2025 Legionella employs the multimodal ubiquitination of Sec22b to modulate SNARE pairing. iScience 0 41669755
2023 It takes a sec(22b) to accrue plasma cells. Immunology and cell biology 0 36789450

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