Affinage

JAM2

Junctional adhesion molecule B · UniProt P57087

Length
298 aa
Mass
33.2 kDa
Annotated
2026-06-10
43 papers in source corpus 24 papers cited in narrative 24 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

JAM2 (JAM-B) is a tight-junction-associated immunoglobulin-superfamily adhesion molecule that seals interendothelial/interepithelial junctions and couples cell-cell adhesion to leukocyte trafficking, myogenesis, and neurovascular integrity (PMID:11053409, PMID:11590146). Its principal binding partner is JAM3 (JAM-C): the JAM-B ectodomain forms high-affinity heterodimers that recruit and stabilize JAM-C in junctional complexes, and JAM-B's first Ig-like fold mediates both this heterotypic interaction and a JAM3-dependent engagement of α4β1 (VLA-4) integrin on lymphocytes (PMID:11590146, PMID:12070135, PMID:16093349). Through serine-phosphorylation-regulated junctional clustering, JAM-2 binds the polarity protein PAR-3 and ZO-1 via PDZ-domain interactions, recruiting them to nascent cell-cell contacts (PMID:12953056). Functionally, JAM-B supports lymphocyte rolling and firm adhesion and promotes leukocyte entry into tissue and the CNS parenchyma without being required for the initial BBB crossing (PMID:19740376, PMID:29920328), and acts in trans with JAM-C to drive myocyte fusion into syncytial muscle fibres (PMID:22180726). In the nervous system JAM-2 is a somatodendritic inhibitory cue that prevents oligodendrocyte myelination of neuronal somata and dendrites (PMID:27499083). Biallelic loss-of-function mutations in JAM2 cause primary familial brain calcification, with truncating alleles abolishing protein and a missense allele (p.W168C) blocking trafficking to the plasma membrane, and the knockout mouse recapitulates the neuropathology, establishing JAM2 as a blood-brain-barrier tight-junction protein required for CNS homeostasis (PMID:31851307, PMID:32142645). JAM-B expression is post-translationally suppressed by TGF-β3 through Smad-dependent ubiquitin-proteasome degradation and ERK/JNK-mediated mRNA destabilization (PMID:25817991).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 2000 Medium

    Established that JAM-2 is a junctional component whose expression actively seals paracellular barriers, defining its baseline role in tight-junction integrity.

    Evidence Real-time video microscopy and permeability assays in JAM-2-transfected monolayers

    PMID:11053409

    Open questions at the time
    • Did not identify binding partners mediating the sealing
    • No in vivo barrier validation
  2. 2001 High

    Identified JAM3 as the heterotypic counter-receptor for JAM2, answering what molecule JAM2 engages on apposed cells and lymphocytes.

    Evidence JAM2-Fc pulldown, static adhesion assays with JAM3-expressing T cells, antibody blocking

    PMID:11590146

    Open questions at the time
    • Affinity and stoichiometry of the heterodimer not quantified
    • Structural basis of binding not resolved
  3. 2002 High

    Showed JAM2 additionally engages α4β1 integrin on leukocytes but only after prior JAM3 binding, and mapped both interactions to the first Ig-like fold, linking adhesion architecture to leukocyte recruitment.

    Evidence Integrin-blocking antibodies, small-molecule inhibitor, JAM3 blocking serum, and JAM2 domain/point mutants in adhesion assays; concurrent immune-cell adhesion characterization

    PMID:11823489 PMID:12070135

    Open questions at the time
    • Conformational change converting JAM2 to an integrin ligand not defined
    • In vivo relevance of integrin engagement not yet tested in this work
  4. 2003 High

    Connected JAM2 adhesion to intracellular polarity machinery by demonstrating phosphorylation-regulated, PDZ-dependent recruitment of PAR-3 and ZO-1, explaining how junctional JAM2 organizes the contact site.

    Evidence Co-immunoprecipitation, PDZ-domain deletion mutants, and immunofluorescence in CHO cells ectopically expressing JAM-2

    PMID:12953056

    Open questions at the time
    • Kinase controlling the regulatory serine phosphorylation not identified
    • Done in ectopic CHO system, not native junctions
  5. 2005 High

    Defined the regulatory logic of the JAM-B/JAM-C heterodimer—JAM-B sequesters JAM-C, and disrupting the pair liberates JAM-C to engage αMβ2 integrin—establishing JAM-B as a gatekeeper of leukocyte adhesion; in vivo blockade reduced leukocyte extravasation in skin.

    Evidence Soluble protein competition, antibody-mediated complex disruption, αMβ2 adhesion assays; murine allergic contact dermatitis blockade

    PMID:16093349 PMID:16297198

    Open questions at the time
    • Trigger for physiological heterodimer disruption in vivo unknown
    • Quantitative affinity differences inferred from competition, not direct binding constants
  6. 2006 High

    Tested whether the embryonic-stem-cell-enriched JAM-B is required for stemness, finding it dispensable for stem cell self-renewal and differentiation, narrowing its functional scope.

    Evidence Jam-B knockout mice with neural and hematopoietic stem cell self-renewal/differentiation assays

    PMID:16914739

    Open questions at the time
    • Does not address adhesion functions of JAM-B in other tissues
    • Possible redundancy with related JAMs not examined
  7. 2009 High

    Resolved the dynamic step of leukocyte trafficking that JAM-B controls, showing it supports both rolling and firm adhesion via α4β1 in skin microvasculature and is required for contact-hypersensitivity sensitization.

    Evidence Intravital microscopy, flow-chamber lymphocyte perfusion over JAM-B, integrin blockade, adoptive transfer

    PMID:19740376

    Open questions at the time
    • Relative contribution of JAM3 versus integrin engagement in vivo not separated
    • Endothelial signaling downstream of JAM-B engagement unknown
  8. 2011 High

    Revealed a developmental, non-immune role: JAM-B and JAM-C must interact in trans between adjacent myoblasts to drive myocyte fusion, defining a requirement for syncytial muscle formation.

    Evidence Heritable zebrafish jamb/jamc mutants, cell transplantation establishing trans requirement, physical interaction analysis

    PMID:22180726

    Open questions at the time
    • Fusogenic machinery downstream of JAM engagement not identified
    • Conservation of myocyte-fusion role in mammals not addressed here
  9. 2014 Medium

    Extended JAM-B/JAM-C adhesion to the bone marrow niche, showing the interaction between HSPCs and stromal/mesenchymal cells is required for homing and reconstitution.

    Evidence Anti-Jam-C blocking antibody, bone marrow reconstitution and homing assays, human cell-type adhesion comparisons

    PMID:24357068

    Open questions at the time
    • JAM-B-side signaling in HSPCs not dissected
    • Single lab, blocking-antibody-based
  10. 2015 High

    Defined how JAM-B levels are controlled, showing TGF-β3 suppresses JAM-B by two parallel routes—Smad-dependent ubiquitin-proteasome degradation and ERK/JNK-driven mRNA destabilization.

    Evidence Pharmacological inhibitors, siRNA against Smad and kinases, Co-IP, mRNA stability assays in Sertoli cells

    PMID:25817991

    Open questions at the time
    • E3 ligase mediating degradation not identified
    • Generality beyond Sertoli cells not established
  11. 2016 Medium

    Identified JAM-2 as a somatodendritic inhibitory myelin-guidance cue, answering how neurons restrict oligodendrocyte myelination to axons.

    Evidence Neuron-oligodendrocyte myelinating co-culture, chemical cross-linking, candidate sequencing

    PMID:27499083

    Open questions at the time
    • Oligodendrocyte-side receptor not defined in this work
    • Downstream inhibitory signaling pathway unknown
  12. 2016 Medium

    Implicated JAM-B/JAM-C adhesion in vascular wall stabilization during fibrogenesis, linking JAM-B-positive endothelium to JAM-C-expressing pericytic stellate cells.

    Evidence Immunohistochemistry, flow cytometry, contractility/migration and tubulogenesis assays with soluble JAM-C; additional Co-IP linking PRL-3 to JAM2 in colon cancer

    PMID:27111582 PMID:27588115

    Open questions at the time
    • PRL-3/JAM2 interaction rests on a single Co-IP with incomplete pathway placement
    • Signaling consequences of vessel-wall JAM-B engagement not mapped
  13. 2018 Medium

    Demonstrated tissue-level consequences of JAM-B, showing its deficiency reduces liver fibrosis independently of leukocyte infiltration and traps inflammatory cells at CNS borders without blocking BBB crossing, refining JAM-B's role to parenchymal entry.

    Evidence JAM-B knockout mice in autoimmune hepatitis and EAE models, soluble JAM-C treatment, adoptive transfer and CNS cell quantification

    PMID:29753567 PMID:29920328

    Open questions at the time
    • Molecular step distinguishing border arrest from parenchymal entry unresolved
    • Cell type providing the JAM-C counter-signal in each context not pinned down
  14. 2020 High

    Established JAM2 as a human disease gene, showing biallelic loss-of-function (truncations abolishing protein; p.W168C blocking membrane trafficking) causes primary familial brain calcification, with the knockout mouse recapitulating the neuropathology.

    Evidence Whole-genome/exome sequencing, homozygosity mapping, mutant protein expression and localization in CHO cells, patient fibroblasts, and jam2 KO mouse neuropathology

    PMID:31851307 PMID:32142645

    Open questions at the time
    • Mechanism linking BBB JAM2 loss to calcification not defined
    • Cell type within the neurovascular unit driving pathology not isolated
  15. 2023 Medium

    Placed JAM2 within a developmental transcriptional program, showing a Pou4f1-Tbr1-Jam2 hierarchy directs formation of orientation-selective retinal ganglion cells.

    Evidence CUT&Tag of Pou4f1 binding, Pou4f1 knockout, enhancer reporter assays

    PMID:38469155

    Open questions at the time
    • Adhesive function of JAM2 in J-RGC wiring not directly tested
    • Downstream effectors of JAM2 in these neurons unknown
  16. 2025 Medium

    Identified a vasculogenic role for the JAM2 ortholog, placing Jam2b downstream of Hand2 and upstream of Etv2 for secondary vascular field progenitor emergence and intestinal vascularization.

    Evidence Zebrafish lineage tracing, double maternal-zygotic jam2a;jam2b mutants, hand2 loss-of-function (preprint)

    PMID:41278682

    Open questions at the time
    • Preprint, not yet peer-reviewed
    • Whether JAM2 acts via adhesion or signaling in progenitor emergence unresolved
    • Mammalian conservation untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • How JAM-B/JAM-C heterodimer disruption is physiologically triggered, and the precise molecular step by which JAM-B licenses leukocyte parenchymal entry and contributes to brain calcification, remain unresolved.
  • No structural model of the JAM-B/JAM-C/integrin switch
  • Downstream signaling from JAM-B engagement uncharacterized
  • Link between BBB tight-junction loss and calcification mechanism unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098631 cell adhesion mediator activity 4 GO:0005198 structural molecule activity 2 GO:0060090 molecular adaptor activity 1
Localization
GO:0005886 plasma membrane 3 GO:0005634 nucleus 1 GO:0005794 Golgi apparatus 1
Pathway
R-HSA-1500931 Cell-Cell communication 3 R-HSA-168256 Immune System 3 R-HSA-1266738 Developmental Biology 2
Partners
ITGA4JAM3PARD3PTP4A3TJP1

Evidence

Reading pass · 24 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 JAM-2 localizes to tight junctional complexes of polarized cells and newly formed cell-cell contacts within minutes, and its expression reduces paracellular permeability of cell monolayers, indicating a role in interendothelial junctional complex sealing. Real-time video microscopy, transfection of JAM-2 cDNA into cell monolayers with permeability assays, immunolocalization The Journal of biological chemistry Medium 11053409
2001 JAM3 is the heterotypic counter-receptor for JAM2; JAM3 ectodomain binds firmly to JAM2-Fc, and JAM3 expressed on T cells mediates JAM2 adhesion, identifying JAM3 as the 43-kDa counter-receptor on lymphocytes. Fc-fusion pulldown (JAM2-Fc capturing JAM3), static adhesion assays with JAM3-expressing cells, polyclonal anti-JAM3 serum blocking experiments The Journal of biological chemistry High 11590146
2002 JAM2 interacts with α4β1 integrin on T cells, but this interaction requires prior heterotypic engagement of JAM2 with JAM3; the first Ig-like fold of JAM2 is sufficient for binding both JAM3 and α4β1, and Asp-82 in the C-D loop is not required for α4β1 binding. Neutralizing integrin antibodies, small-molecule integrin inhibitor (TBC 772), JAM3 blocking serum, JAM2 domain/point mutants in adhesion assays The Journal of biological chemistry High 12070135
2002 VE-JAM/JAM2 mediates adhesion to T cells, NK cells, and dendritic cells through heterotypic interaction with JAM3 expressed on those immune cells. Cell adhesion assays, antibody blocking, JAM3 cloning and functional characterization Journal of immunology Medium 11823489
2003 JAM-2 directly associates with the cell polarity protein PAR-3 via the first PDZ domain of PAR-3; JAM-2 also associates with ZO-1 in a PDZ domain-dependent manner. Junctional clustering of JAM-2 (regulated by serine phosphorylation) recruits endogenous PAR-3 and ZO-1 to cell-cell contacts in CHO cells. Co-immunoprecipitation, ectopic expression of JAM-2 in CHO cells, immunofluorescence localization, PDZ domain deletion mutants Journal of cell science High 12953056
2005 JAM-B (JAM2) and JAM-C undergo heterophilic interaction at cell-cell contacts; JAM-B recruits and stabilizes JAM-C in junctional complexes. Soluble JAM-B dissociates JAM-C homodimers to form JAM-B/JAM-C heterodimers, indicating higher affinity of JAM-C for JAM-B than for itself. Disrupting JAM-B/JAM-C heterodimers with anti-JAM-C antibodies liberates JAM-C to the apical surface, enabling interaction with the leukocyte counter-receptor αMβ2 integrin. Cell-cell contact co-localization, soluble protein competition assays, antibody-mediated complex disruption, αMβ2-dependent leukocyte adhesion assays Molecular biology of the cell High 16093349
2005 In vivo blockade of JAM-B (using neutralizing antibodies) reduces leukocyte extravasation into the skin and attenuates allergic contact dermatitis; combined JAM-B and JAM-C blockade produces additive inhibition, indicating distinct functions for each molecule in cutaneous inflammation. In vivo antibody blockade in murine allergic contact dermatitis model, histology, enzyme activity assays The Journal of investigative dermatology Medium 16297198
2006 Jam-B (JAM2) is specifically expressed in undifferentiated embryonic stem cells, but Jam-B knockout mice are fertile with no overt developmental defects, and neural and hematopoietic stem cells from knockout mice show normal self-renewal and differentiation, demonstrating JAM-B is dispensable for stem cell identity. DNA microarray expression profiling, Jam-B homozygous knockout mouse generation, stem cell self-renewal and differentiation assays Molecular and cellular biology High 16914739
2009 JAM-B supports lymphocyte rolling and firm adhesion through interaction with α4β1 (VLA-4) integrin; blocking JAM-B in vivo reduces rolling interactions in skin microvasculature and impairs sensitization phase of contact hypersensitivity. Intravital microscopy, dynamic flow chamber T-lymphocyte perfusion over JAM-B-coated slides, integrin-blocking antibodies, adoptive transfer experiments Immunology High 19740376
2011 Zebrafish jamb and jamc are essential for myocyte fusion to form syncytial muscle fibres; the encoded receptors physically interact and must engage in trans between neighbouring cells for fusion to occur. Loss of either gene results in mononuclear fast-twitch muscle fibres without other overt defects. Heritable zebrafish mutations, in vivo muscle development analysis, cell transplantation (trans interaction requirement), dynamic co-expression analysis PLoS biology High 22180726
2014 Jam-B/Jam-C interaction between hematopoietic stem/progenitor cells (HSPC) and bone marrow stromal cells is required for HSPC homing and reconstitution; blocking Jam-C with a monoclonal antibody inhibits reconstitution and progenitor homing in a Jam-B-dependent manner and induces HSPC mobilization. The functional adhesive interaction between JAM-B and JAM-C exists between human HSPC and mesenchymal stem cells but not endothelial cells or osteoblasts. Blocking monoclonal antibody against Jam-C, bone marrow reconstitution assays after irradiation, HSPC mobilization measurements, adhesion assays between human cell types Stem cells Medium 24357068
2015 TGF-β3 suppresses JAM-B expression via two mechanisms: (1) post-translational degradation through the ubiquitin-proteasome pathway requiring Smad signaling, and (2) mRNA destabilization requiring ERK1/2 and p54 JNK activation. Blockade of the ubiquitin-proteasome pathway abrogates TGF-β3-induced loss of JAM-B at cell-cell interfaces in Sertoli cells. Pharmacological inhibitors, siRNA knockdown of Smad and kinases, co-immunoprecipitation, mRNA stability assay, immunofluorescence staining Biochimica et biophysica acta High 25817991
2016 JAM-2 is expressed somatodendritically in neurons and acts as an inhibitory myelin-guidance molecule that prevents oligodendrocyte myelination of the somatodendritic compartment; disruption of dynamic neuron-oligodendrocyte signaling leads to aberrant myelination of somata and dendrites. Purified spinal cord neuron-oligodendrocyte myelinating co-culture, chemical cross-linking, next-generation sequencing, candidate profiling Neuron Medium 27499083
2016 PRL-3 (PTP4A3) physically interacts with JAM2 in colon cancer cells, as shown by co-immunoprecipitation and immunofluorescence; PRL-3 expression affects cell motility, spreading speed, and cell-matrix adhesion. Co-immunoprecipitation, immunofluorescence, cell wounding assay, cell spread assay, cell-matrix adhesion assay Oncology letters Low 27588115
2016 During hepatic fibrogenesis, JAM-C is de novo expressed on myofibroblastic hepatic stellate cells, linking them as pericytes to JAM-B-positive endothelial cells; soluble JAM-C blocks stellate cell contractility, increases motility, and reduces endothelial tubulogenesis and endothelial-stellate cell interaction, indicating JAM-B/JAM-C interaction stabilizes vessel walls. Immunohistochemistry, flow cytometry, contractility and migration assays, endothelial tubulogenesis assay, soluble JAM-C treatment Cell adhesion & migration Medium 27111582
2018 JAM-B deficiency in mice (JAM-B−/−) ameliorates autoimmune-mediated liver fibrosis in a model of autoimmune hepatitis, and soluble recombinant JAM-C also reduces fibrosis; this effect is independent of leukocyte infiltration, suggesting JAM-B/JAM-C interactions directly contribute to fibrotic remodeling rather than through leukocyte recruitment. JAM-B knockout mice, autoimmune hepatitis mouse model, soluble recombinant JAM-C treatment, histological quantification of fibrosis and leukocyte infiltration Journal of autoimmunity Medium 29753567
2018 In JAM-B−/− mice subjected to EAE, inflammatory cells accumulate in leptomeningeal and perivascular spaces but fail to enter the CNS parenchyma, ameliorating EAE. JAM-B is not required for CD4+ T-cell arrest or extravasation across the BBB endothelium, but its absence traps cells at CNS border zones, indicating JAM-B facilitates parenchymal entry rather than initial BBB crossing. JAM-B knockout mice, EAE induction with MOG peptide, adoptive transfer of CD4+ T cells, immunofluorescence, flow cytometry of CNS infiltrating cells Brain, behavior, and immunity Medium 29920328
2020 Biallelic loss-of-function mutations in JAM2 cause primary familial brain calcification (PFBC); truncating mutations (p.L48*, p.M1?) abolish protein expression, and the p.W168C missense mutation prevents JAM2 protein translocation to the plasma membrane, implicating JAM2 in neurovascular unit integrity. Whole genome sequencing, homozygosity mapping, Western blot of mutant proteins in transfected CHO cells, immunofluorescence of mutant protein localization Brain : a journal of neurology High 31851307
2020 Biallelic JAM2 variants cause loss of JAM2 mRNA expression and absence of JAM2 protein in patient fibroblasts (loss-of-function mechanism); the jam2 complete knockout mouse recapitulates the human PFBC phenotype with vacuolation, reactive astrogliosis, and neuronal density reduction, establishing JAM2 as a blood-brain barrier tight-junction protein required for CNS homeostasis. Exome sequencing with homozygosity mapping, patient fibroblast mRNA and protein expression analysis, jam2 KO mouse neuropathology American journal of human genetics High 32142645
2020 JAM-B silencing in pancreatic cancer cells reduces cell migration and invasion, and decreases expression of c-Src and MMP9, placing JAM-B upstream of the c-Src/MMP9 signaling pathway in pancreatic cancer invasion. shRNA-mediated JAM-B silencing, scratch wound assays, Transwell invasion assays, subcutaneous xenograft mouse model, immunohistochemistry for c-Src and MMP9 Journal of Cancer Low 32231730
2022 Lactobacillus johnsonii GAPDH (moonlighting surface protein) physically binds JAM-2 on mouse gut epithelial cells; this interaction is associated with repair of damaged tight junctions and upregulation of tight junction genes in Caco-2 cells. Affinity resin pulldown of gut surface proteins, protein identification by mass spectrometry, Caco-2 cell barrier repair assay, RNA sequencing Food & function Low 36069670
2022 In leukocytes, JAM-B protein localizes to the cytoplasm, Golgi apparatus, and nucleus (around ring-shaped structures); nuclear localization occurs via the classical importin-α/β pathway mediated through JAM-B nuclear localization and export signals. Under inflammatory stimuli, JAM-B transcription is regulated via NF-κB-dependent pathways, and at the post-translational level JAM-B is regulated by ubiquitin-proteasome pathways involving APC/C (ubiquitination) and HAUSP/USP7 (de-ubiquitination). Immunoassays, qPCR, pharmacological inhibitors of importin pathway and NF-κB signaling, proteasome inhibitors International journal of molecular sciences Low 35955781
2023 A Pou4f1-Tbr1-Jam2 transcriptional hierarchy controls formation of JAM2-expressing orientation-selective retinal ganglion cells (J-RGCs); Pou4f1 directly binds regulatory elements of both Tbr1 and Jam2 (identified by CUT&Tag), and Pou4f1 is required for expression of Tbr1 and Jam2 in J-RGCs. CUT&Tag chromatin profiling of Pou4f1 binding sites, genetic loss-of-function (Pou4f1 knockout), reporter gene assays for enhancer activity Frontiers in ophthalmology Medium 38469155
2025 In zebrafish, Jam2b (ortholog of human JAM2) functions downstream of the transcription factor Hand2 and is required for emergence of secondary vascular field (SVF) endothelial progenitors that give rise to intestinal vasculature; double maternal-zygotic jam2a;jam2b mutants show greatly reduced SVF cells and defective intestinal vasculature. Hand2 is required to induce Jam2b expression and the downstream vasculogenic transcription factor Etv2/Etsrp. Time-lapse imaging, jam2b:Cre lineage tracing, double maternal-zygotic jam2a;jam2b mutant zebrafish, hand2 loss-of-function, etv2 expression analysis bioRxivpreprint Medium 41278682

Source papers

Stage 0 corpus · 43 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity. Journal of cell science 204 12953056
2000 JAM-2, a novel immunoglobulin superfamily molecule, expressed by endothelial and lymphatic cells. The Journal of biological chemistry 189 11053409
2001 Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. The Journal of biological chemistry 172 11590146
2002 JAM2 interacts with alpha4beta1. Facilitation by JAM3. The Journal of biological chemistry 140 12070135
2002 Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2 interacts with T, NK, and dendritic cells through JAM 3. Journal of immunology (Baltimore, Md. : 1950) 118 11823489
2005 Dual interaction of JAM-C with JAM-B and alpha(M)beta2 integrin: function in junctional complexes and leukocyte adhesion. Molecular biology of the cell 98 16093349
2016 Somatodendritic Expression of JAM2 Inhibits Oligodendrocyte Myelination. Neuron 85 27499083
2020 Biallelic loss-of-function mutations in JAM2 cause primary familial brain calcification. Brain : a journal of neurology 80 31851307
2011 Jamb and jamc are essential for vertebrate myocyte fusion. PLoS biology 80 22180726
2005 Junctional adhesion molecules (JAM)-B and -C contribute to leukocyte extravasation to the skin and mediate cutaneous inflammation. The Journal of investigative dermatology 76 16297198
2020 Bi-allelic JAM2 Variants Lead to Early-Onset Recessive Primary Familial Brain Calcification. American journal of human genetics 73 32142645
2004 Enzymatic properties and nucleotide and amino acid sequences of a thermostable beta-agarase from the novel marine isolate, JAMB-A94. Bioscience, biotechnology, and biochemistry 57 15170112
2005 High-level expression of a neoagarobiose-producing beta-agarase gene from Agarivorans sp. JAMB-A11 in Bacillus subtilis and enzymic properties of the recombinant enzyme. Biotechnology and applied biochemistry 52 15307821
2006 Putative "stemness" gene jam-B is not required for maintenance of stem cell state in embryonic, neural, or hematopoietic stem cells. Molecular and cellular biology 44 16914739
2005 Sequence of the gene for a high-alkaline mannanase from an alkaliphilic Bacillus sp. strain JAMB-750, its expression in Bacillus subtilis and characterization of the recombinant enzyme. Extremophiles : life under extreme conditions 40 15999223
2018 MicroRNA-374b inhibits cervical cancer cell proliferation and induces apoptosis through the p38/ERK signaling pathway by binding to JAM-2. Journal of cellular physiology 38 29575013
2009 Junctional adhesion molecule (JAM)-B supports lymphocyte rolling and adhesion through interaction with alpha4beta1 integrin. Immunology 38 19740376
2010 Hyper-production and characterization of the ι-carrageenase useful for ι-carrageenan oligosaccharide production from a deep-sea bacterium, Microbulbifer thermotolerans JAMB-A94T, and insight into the unusual catalytic mechanism. Marine biotechnology (New York, N.Y.) 37 20686828
2014 Function of Jam-B/Jam-C interaction in homing and mobilization of human and mouse hematopoietic stem and progenitor cells. Stem cells (Dayton, Ohio) 34 24357068
2022 Lactobacillus johnsonii enhances the gut barrier integrity via the interaction between GAPDH and the mouse tight junction protein JAM-2. Food & function 29 36069670
2018 Lack of junctional adhesion molecule (JAM)-B ameliorates experimental autoimmune encephalomyelitis. Brain, behavior, and immunity 25 29920328
2015 Transforming growth factor-β3 regulates cell junction restructuring via MAPK-mediated mRNA destabilization and Smad-dependent protein degradation of junctional adhesion molecule B (JAM-B). Biochimica et biophysica acta 25 25817991
2018 Junctional adhesion molecules JAM-B and JAM-C promote autoimmune-mediated liver fibrosis in mice. Journal of autoimmunity 21 29753567
2016 Murine junctional adhesion molecules JAM-B and JAM-C mediate endothelial and stellate cell interactions during hepatic fibrosis. Cell adhesion & migration 18 27111582
2016 The role of JAM-B in cancer and cancer metastasis (Review). Oncology reports 16 27121546
2018 Genetic Mutations in jamb, jamc, and myomaker Revealed Different Roles on Myoblast Fusion and Muscle Growth. Marine biotechnology (New York, N.Y.) 15 30467785
2018 MicroRNA-374b inhibits the tumor growth and promotes apoptosis in non-small cell lung cancer tissue through the p38/ERK signaling pathway by targeting JAM-2. Journal of thoracic disease 13 30416798
2012 JAM-2 siRNA intracellular delivery and real-time imaging by proton-sponge coated quantum dots. Journal of materials chemistry. B 12 32260769
2020 The JAM-B/c-src/MMP9 pathway is associated with progression and regulates the invasion of pancreatic cancer. Journal of Cancer 9 32231730
2016 PRL-3 promotes cell adhesion by interacting with JAM2 in colon cancer. Oncology letters 9 27588115
2014 Inhibition of glioma proliferation and migration by magnetic nanoparticle mediated JAM-2 silencing. Journal of materials chemistry. B 9 32261795
2016 Differential mouse-strain specific expression of Junctional Adhesion Molecule (JAM)-B in placental structures. Cell adhesion & migration 8 26914234
2020 Regulation of JAM2 Expression in the Lungs of Streptozotocin-Induced Diabetic Mice and Human Pluripotent Stem Cell-Derived Alveolar Organoids. Biomedicines 7 32932992
2021 JAM2: A New Culprit at the Pathophysiology of Primary Familial Brain Calcification. Journal of molecular neuroscience : MN 5 33743113
2024 JAM2 variants can be more common in primary familial brain calcification (PFBC) cases than those appear; may be due to a founder mutation. Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology 4 38441788
2023 Pou4f1-Tbr1 transcriptional cascade controls the formation of Jam2-expressing retinal ganglion cells. Frontiers in ophthalmology 4 38469155
2019 MicroRNA-374 targets JAM-2 regulates the growth and metastasis of human pancreatic cancer cells. American journal of translational research 4 31737197
2025 Lack of junctional adhesion molecule (JAM)-B traps CD8 T cells in CNS border zones and ameliorates autoimmune neuroinflammation. Acta neuropathologica communications 3 40420242
2025 Aberrant Expression of JAM2 Inhibits Invasion and Migration in Lung Adenocarcinoma. Cancer reports (Hoboken, N.J.) 1 39838844
2011 Jamb and jamc muscle in on myoblast fusion. PLoS biology 1 22180727
2025 Clinical Significance of JAM-2 Expression in the Vaginal Wall Tissues of Patients With Pelvic Organ Prolapse. Journal of cellular and molecular medicine 0 40159633
2025 Jam2 Signaling Functions Downstream of Hand2 To Initiate The Formation Of Organ-Specific Vascular Progenitors In Zebrafish. bioRxiv : the preprint server for biology 0 41278682
2022 Transcriptional and Post-Translational Regulation of Junctional Adhesion Molecule-B (JAM-B) in Leukocytes under Inflammatory Stimuli. International journal of molecular sciences 0 35955781

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