Affinage

DLG3

Disks large homolog 3 · UniProt Q92796

Length
817 aa
Mass
90.3 kDa
Annotated
2026-04-28
58 papers in source corpus 26 papers cited in narrative 26 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DLG3 (SAP102) is a MAGUK-family postsynaptic scaffold protein that organizes glutamate receptor trafficking, clustering, and downstream signaling at excitatory synapses, with additional roles in epithelial polarity and growth suppression. SAP102 binds NMDA receptor GluN2B subunits through both PDZ-dependent and PDZ-independent N-terminal interactions, mediating synaptic delivery of NMDARs during early synaptogenesis and activity-dependent clearance of GluN2B-containing receptors, while also regulating AMPAR trafficking through a cornichon-2-dependent pathway (PMID:8780649, PMID:21209193, PMID:23103165, PMID:19104036, PMID:30067114). Its synaptic residence is dynamically controlled by CK2 phosphorylation of Ser632 and JNK3 phosphorylation, and it recruits signaling effectors including Pyk2 (via SH3 domain), EphB2/Kalirin-7/PAK, and the exocyst subunit Sec8 (via PDZ2) to coordinate actin remodeling and synapse formation (PMID:29282697, PMID:38582451, PMID:12576483, PMID:23486974, PMID:37849738). In epithelial cells, DLG3 recruits Nedd4/Nedd4-2 E3 ligases through PPxY motifs, undergoes monoubiquitination required for apical membrane targeting and tight junction formation, and can suppress cell proliferation through PDZ-domain-dependent downregulation of β-catenin (PMID:21920314, PMID:10797259).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1996 High

    Establishing that SAP102 is a direct physical link between the NMDA receptor complex and the postsynaptic scaffold answered the fundamental question of how NMDARs are anchored at synapses, revealing PDZ-domain-mediated binding to the NR2B C-terminal tail as the molecular basis.

    Evidence Co-immunoprecipitation from rat brain synaptosomes, recombinant PDZ domain binding assays, and overlay assays with synthetic peptides

    PMID:8702950 PMID:8780649

    Open questions at the time
    • Stoichiometry of SAP102–NMDAR complex unknown
    • In vivo functional consequence of disrupting this interaction not tested
    • Whether other MAGUK family members are redundant at this stage was unclear
  2. 1997 Medium

    Demonstrating that SAP102 functionally substitutes for the Drosophila Dlg tumor suppressor and interacts with APC established that its scaffolding function is evolutionarily conserved and extends beyond receptor anchoring to growth regulation.

    Evidence Genetic complementation of Drosophila dlg-1 mutants; yeast two-hybrid and in vitro binding with APC

    PMID:9152008 PMID:9188857

    Open questions at the time
    • APC interaction not validated endogenously in mammalian neurons
    • Relevance of tumor suppression to normal neuronal SAP102 function unclear
  3. 1999 High

    Identification of Ca²⁺/calmodulin binding (Kd ~44 nM) near the SH3 domain and the competitive regulator nedasin revealed that SAP102 scaffolding is subject to calcium-dependent conformational regulation and competitive interference during synaptogenesis.

    Evidence Surface plasmon resonance, yeast two-hybrid, and in vitro competition assays

    PMID:10026200 PMID:10542258

    Open questions at the time
    • Physiological consequences of calmodulin binding on SAP102 scaffolding in neurons not shown
    • Nedasin's in vivo role in regulating SAP102–NMDAR not confirmed
  4. 2003 High

    Showing that Pyk2 binds the SAP102 SH3 domain—regulated by intramolecular SH3–GK interaction—answered how tyrosine kinase signaling is recruited to the NMDAR complex and revealed an autoinhibitory conformational switch in SAP102.

    Evidence Reciprocal co-immunoprecipitation, pulldown with deletion mutants

    PMID:12576483

    Open questions at the time
    • Functional consequence of Pyk2 recruitment through SAP102 on NMDAR signaling not directly measured
    • Structural basis of intramolecular SH3–GK regulation not resolved
  5. 2005 High

    Discovery that mPins promotes SAP102 and NMDAR trafficking to the plasma membrane, with mPins knockdown reducing dendritic SAP102 and surface NMDARs, established a dedicated trafficking pathway for the SAP102–NMDAR complex.

    Evidence Co-immunoprecipitation, siRNA knockdown, and dominant-negative constructs in neurons

    PMID:16299499

    Open questions at the time
    • Mechanism by which mPins drives vesicular transport of SAP102 undefined
    • Whether mPins acts on SAP102 independently of other MAGUKs not determined
  6. 2008 High

    Genetic epistasis in PSD-95/PSD-93 double-knockout mice demonstrated that SAP102 is the predominant MAGUK mediating both AMPAR and NMDAR trafficking during synaptogenesis, with PSD-95 assuming these roles after synapses mature.

    Evidence In utero electroporation, dual whole-cell electrophysiology, and knockout mice

    PMID:19104036

    Open questions at the time
    • Molecular basis of the developmental handoff from SAP102 to PSD-95 unknown
    • Whether SAP102 retains any unique function at mature synapses not fully resolved
  7. 2011 High

    Two breakthroughs redefined SAP102 function: discovery of a PDZ-independent N-terminal NR2B-binding site regulated by alternative splicing, and demonstration that DLG3 monoubiquitination by Nedd4/Nedd4-2 via PPxY motifs drives apical membrane targeting and tight junction formation in epithelia.

    Evidence Co-IP with shRNA knockdown and spine morphology in neurons; mass spectrometry complex purification, PPxY mutagenesis, and KO mouse for epithelial phenotype

    PMID:21209193 PMID:21920314

    Open questions at the time
    • How the N-terminal and PDZ-mediated interactions with NR2B are coordinated at a single synapse is unknown
    • Whether monoubiquitination similarly regulates SAP102 in neurons not tested
  8. 2012 High

    Identification of specific GluN2B residues required for non-PDZ binding to SAP102 established that SAP102 mediates synaptic clearance of GluN2B-NMDARs through this second binding mode, explaining why PDZ-binding-deficient receptors are still regulated.

    Evidence Site-directed mutagenesis of GluN2B, SAP102 siRNA, surface biotinylation

    PMID:23103165

    Open questions at the time
    • Whether clearance occurs via endocytosis or lateral diffusion not resolved
    • Structural basis of non-PDZ interaction not determined
  9. 2013 High

    Demonstration that SAP102 scaffolds an EphB2/Kalirin-7/PAK signaling complex in neonatal cortex, with SAP102 loss blocking ephrinB-induced actin reorganization and synapse formation, identified a specific developmental signaling axis organized by SAP102.

    Evidence Lentiviral shRNA knockdown, co-immunoprecipitation, PAK activity measurement in cortical neurons

    PMID:23486974

    Open questions at the time
    • Whether EphB signaling through SAP102 is independent of its NMDAR scaffolding role unclear
    • Downstream PAK substrates mediating synaptogenesis not identified
  10. 2017 High

    Identifying CK2-mediated phosphorylation of Ser632 as a regulator of SAP102 synaptic enrichment and mobility established that activity-dependent kinase signaling tunes SAP102 residence time at synapses.

    Evidence In vitro kinase assay, phosphomutant analysis, FRAP in cultured neurons

    PMID:29282697

    Open questions at the time
    • In vivo relevance of Ser632 phosphorylation to synaptic plasticity not tested
    • Other kinases that may co-regulate SAP102 localization not surveyed
  11. 2023 High

    A 2.5 Å crystal structure of Sec8 C-terminus bound to SAP102 PDZ2 revealed how the exocyst complex interfaces with the MAGUK scaffold, providing the first structural view of an SAP102 PDZ domain interaction and defining a 14-residue spacer required for binding.

    Evidence X-ray crystallography, biochemical binding assays, deletion mutagenesis

    PMID:37849738

    Open questions at the time
    • Functional consequence of Sec8–SAP102 interaction for receptor exocytosis not demonstrated
    • No full-length SAP102 structure available
  12. 2024 High

    JNK3 was identified as a direct SAP102 kinase that regulates dendritic spine dynamics and cooperates with SAP102 to traffic kainate receptor GluK2 to the surface, extending SAP102's scaffolding role beyond NMDA and AMPA receptors to a third ionotropic glutamate receptor class.

    Evidence In vitro kinase assay, live-cell imaging, pharmacological JNK inhibition with surface GluK2 measurement

    PMID:38582451

    Open questions at the time
    • JNK3 phosphorylation site(s) on SAP102 not mapped
    • Whether GluK2 trafficking by SAP102 is PDZ-dependent or uses the N-terminal binding mode unknown
  13. 2024 Medium

    Super-resolution imaging revealed that SAP102 forms subsynaptic nanoclusters distinct from PSD-95 nanodomains, with differential presynaptic Munc13-1 alignment, establishing that MAGUKs create heterogeneous signaling subcompartments within single synapses.

    Evidence DNA-PAINT super-resolution microscopy with nanocluster analysis in rat neurons

    PMID:38777601

    Open questions at the time
    • Functional significance of SAP102-specific nanodomains for receptor signaling not tested
    • Whether nanocluster composition changes with development or plasticity unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: the structural basis of full-length SAP102 autoinhibition and how multiple binding modes (PDZ, N-terminal, SH3) are simultaneously coordinated; the precise phosphorylation sites targeted by JNK3; and whether SAP102's epithelial polarity function involves the same molecular interactions as its synaptic scaffolding role.
  • No full-length structural model of SAP102
  • Relationship between neuronal and epithelial functions mechanistically undefined
  • In vivo consequences of SAP102 nanocluster organization for synaptic transmission not established

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 6 GO:0005198 structural molecule activity 3
Localization
GO:0005886 plasma membrane 4 GO:0005634 nucleus 1 GO:0005829 cytosol 1
Pathway
R-HSA-112316 Neuronal System 9 R-HSA-9609507 Protein localization 4 R-HSA-1266738 Developmental Biology 3 R-HSA-162582 Signal Transduction 3 R-HSA-1500931 Cell-Cell communication 1
Complex memberships
EphB2/Kalirin-7/PAK complexNMDAR-MAGUK postsynaptic complex

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1996 SAP102 (DLG3) directly interacts with NMDA receptor complex in vivo; all three PDZ domains of SAP102 bind the cytoplasmic tail of NR2B subunit in vitro, and anti-NMDA receptor antibodies co-immunoprecipitate SAP102 from rat brain synaptosomes. Co-immunoprecipitation from rat brain synaptosomes; recombinant protein pulldown; in vitro PDZ domain binding assays Neuron High 8702950 8780649
1996 SAP102 specifically binds the last 20 amino acids of the NR2 subunit C-terminal tail; no interaction was detected with the NR1a intracellular C-terminal tail or with AMPA receptor subunit GluR1. Hexahistidine fusion protein overlay assay; synthetic peptide binding; co-immunoprecipitation from cortical synaptic plasma membranes The Journal of biological chemistry High 8702950
1997 SAP102 can functionally substitute for Drosophila DlgA tumor suppressor: heterologous neuronal expression of SAP102 suppresses tumor formation and restores synaptic bouton structure in dlg-1 mutant flies, indicating conserved presynaptic scaffolding function. Heterologous expression in Drosophila dlg-1 mutants; morphological analysis of neuromuscular junctions Mechanisms of development Medium 9152008
1997 NE-dlg/SAP102 interacts with the carboxyl-terminal region of the APC tumor suppressor protein, suggesting a role in regulating cell proliferation. Yeast two-hybrid screening; in vitro binding assay Oncogene Medium 9188857
1999 SAP102 interacts with calmodulin in a Ca2+-dependent manner via a basic alpha-helix region near the SH3 domain (Kd ~44 nM); Ca2+/calmodulin binding to SAP102 enables interaction with the GUK-like domain of PSD-95/SAP90, but does not alter SAP102 PDZ domain binding to NR2B. Surface plasmon resonance; yeast two-hybrid; pulldown assay; mutagenesis The Journal of biological chemistry High 10026200
1999 SAP102 interacts with nedasin (p51), a novel amidohydrolase-related protein predominantly expressed in neuronal cell bodies; nedasin competitively interferes with the SAP102–NR2B interaction in vitro, and may regulate receptor clustering during synaptogenesis. Yeast two-hybrid; co-immunoprecipitation; in vitro competition assay The Journal of biological chemistry Medium 10542258
2000 NE-dlg/SAP102 overexpression in proliferating cancer cells induces growth suppression, impairment of cell adhesion, and down-regulation of beta-catenin independent of APC mutation; the PDZ domains are essential for these effects. Overexpression in cancer cell lines; cell proliferation and adhesion assays; PDZ domain mutagenesis International journal of cancer Medium 10797259
2001 SAP102 is detected at postsynaptic densities of asymmetric synapses on spines, as well as along presynaptic membranes, axonal cytoplasm, and dendritic shafts, suggesting dual roles in anchoring receptors at synapses and regulating receptor shuttling. Electron microscopic immunocytochemistry (EM-ICC) with quantitative analysis Synapse (New York, N.Y.) Medium 11309840
2003 The tyrosine kinase Pyk2 is recruited to the NMDA receptor complex via the SH3 domains of SAP102 and PSD-95; Pyk2 proline-rich regions bind SAP102 SH3 domain, and this binding is regulated by an intramolecular SH3–GK domain interaction in SAP102. Co-immunoprecipitation; pulldown assays; colocalization; deletion mutant analysis The Journal of biological chemistry High 12576483
2005 mPins interacts with SAP102 and functions in formation of the NMDAR-MAGUK complex; mPins enhances trafficking of SAP102 and NMDARs to the plasma membrane, and siRNA knockdown of mPins decreases SAP102 in dendrites and reduces NMDAR surface expression. Co-immunoprecipitation; siRNA knockdown; dominant-negative constructs; immunofluorescence Nature cell biology High 16299499
2008 SAP102 mediates synaptic trafficking of both AMPA and NMDA receptors during synaptogenesis; after synaptogenesis, PSD-95 assumes these functions. In PSD-95/PSD-93 double-KO mice, the developmental NR2B-to-NR2A switch fails, and PSD-95 (not SAP102) rescues it. In utero electroporation; dual whole-cell electrophysiology; genetic knockout mice Proceedings of the National Academy of Sciences of the United States of America High 19104036
2011 SAP102 contains a novel NR2B-binding site in its N-terminal domain that is PDZ-independent and regulated by alternative splicing; the N-terminal insert splice variant promotes dendritic spine lengthening and synapse formation at long spines in an NMDA receptor activity-dependent manner. Co-immunoprecipitation; knockdown with shRNA; morphological analysis of dendritic spines; NMDA receptor blockade The Journal of neuroscience High 21209193
2011 Dlg3/SAP102 contributes to apical-basal polarity and epithelial tight junction formation; Dlg3 recruits E3 ubiquitin ligases Nedd4 and Nedd4-2 through its PPxY motifs, leading to Dlg3 monoubiquitination that is required for its apical membrane recruitment and tight junction consolidation. Complex purification by mass spectrometry; co-immunoprecipitation; mouse knockout; PPxY motif mutagenesis; ubiquitination assay Developmental cell High 21920314
2012 SAP102 mediates synaptic clearance of GluN2B-containing NMDARs via a non-PDZ interaction; two critical residues on GluN2B are responsible for non-PDZ binding to SAP102, and mutation of these residues or SAP102 knockdown rescues defective surface and synaptic expression of PDZ-binding-deficient GluN2B. Site-directed mutagenesis of GluN2B; siRNA knockdown of SAP102; surface biotinylation; immunofluorescence Cell reports High 23103165
2012 SAP102 binds to the C-terminal part of neurobeachin (containing DUF, PH, BEACH, and WD40 domains); a point mutation in the PH domain of neurobeachin that disrupts PH–BEACH interaction abolishes SAP102 binding. Mass spectrometry from mouse brain; Co-IP in heterologous cells; domain deletion and point mutagenesis PloS one Medium 22745750
2013 SAP102 regulates cortical synapse development through EphB and PAK signaling: SAP102 co-immunoprecipitates EphB2 and Kalirin-7 from neonatal cortex; SAP102 knockdown reduces EphB surface expression, prevents ephrinB-induced actin reorganization, synapse formation, and synaptic AMPAR trafficking, and downregulates PAK activity. Lentiviral shRNA knockdown; co-immunoprecipitation; surface receptor expression assay; immunofluorescence; PAK activity measurement The Journal of neuroscience High 23486974
2014 SAP102 interacts with the A2A adenosine receptor C-terminus via its SH3–GK domain fragment; SAP102 overexpression prevents agonist-induced confinement of A2A receptor to slow-mobility compartments, and a mutated A2A receptor (DVELL→RVRAA) is insensitive to SAP102 action. Co-immunoprecipitation; single-particle tracking; hidden Markov model analysis; C-terminal deletion mutants The Journal of biological chemistry Medium 24509856
2015 Synaptic localization of SAP102 is regulated by C-terminal alternative splicing: the I2 splice variant (insert between SH3 and GK domains) is highly enriched at dendritic spines; knockdown of I2-containing SAP102 isoforms differentially affects NMDAR surface expression in a GluN2 subunit-specific manner. Alternative splicing analysis; shRNA knockdown; surface NMDAR expression by immunofluorescence; intramolecular SH3-GK interaction assay The Journal of biological chemistry Medium 25555912
2016 SAP102 knockout in mice causes reduced thalamocortical axon innervation of somatosensory cortex and a transient acceleration of NMDA receptor kinetics during the critical period, without reducing GluN2B-mediated synaptic transmission; after the critical period, TC connectivity divergence is reduced. Dlg3 knockout mouse; electrophysiology; thalamocortical axon tracing Human molecular genetics Medium 27466188
2017 SAP102 synaptic targeting is regulated by phosphorylation of Ser632 (within the C-terminal alternatively spliced region) by casein kinase II (CK2); Ser632 phosphorylation increases synaptic enrichment and decreases SAP102 mobility, while elevated synaptic activity suppresses Ser632 phosphorylation and reduces synaptic SAP102. In vitro kinase assay; phospho-specific mutagenesis; FRAP; immunofluorescence in neurons Molecular neurobiology High 29282697
2018 SAP102 regulates synaptic AMPAR function through a CNIH-2 (cornichon-2)-dependent mechanism; SAP102 rescues AMPAR eEPSCs following PSD-95 knockdown, increases AMPAR mEPSC decay time, and this rescue requires the auxiliary AMPAR subunit cornichon-2. Molecular replacement (cell-restricted shRNA + rescue expression); whole-cell electrophysiology; cornichon-2 knockdown Journal of neurophysiology Medium 30067114
2020 MIAT lncRNA promotes methylation of CpG islands in the DLG3 promoter by binding DNMT1, DNMT3A, and DNMT3B; MIAT silencing upregulates DLG3, which then binds MST2 and regulates LATS1, preventing nuclear YAP translocation and activating the Hippo signaling pathway to suppress breast cancer progression. MS-PCR; RIP assay; co-immunoprecipitation (DLG3–MST2); in vitro and in vivo functional assays Cellular signalling Medium 32593652
2023 COP1 E3 ubiquitin ligase binds DLG3 protein and promotes its ubiquitination; COP1 knockdown inhibits glioma cell proliferation, invasion, and migration, and DLG3 silencing reverses this inhibition, placing DLG3 downstream of COP1. Co-immunoprecipitation; ubiquitination assay with MG132; shRNA knockdown; functional rescue experiments Neurological research Medium 37356109
2023 Sec8 preferentially binds PDZ2 of SAP102 (over PDZ1 and PDZ3) via its C-terminal ITTV motif; crystal structure of Sec8 C-terminus at 2.5 Å resolution reveals an unusually long helix with a 14-residue spacer bridging the ITTV motif to the Sec8 core, required for SAP102 binding. X-ray crystallography (2.5 Å); biochemical binding assays; deletion mutagenesis of spacer Frontiers in cell and developmental biology High 37849738
2024 JNK3 directly phosphorylates SAP102 and negatively regulates SAP102 dynamics at dendritic spines; SAP102 and JNK3 cooperate in trafficking kainate receptor subunit GluK2 to the cell membrane, and JNK inhibition reduces GluK2 surface expression in a SAP102-dependent manner. In vitro kinase assay; live-cell imaging; biochemical fractionation; pharmacological JNK inhibition; surface receptor expression assay The Journal of biological chemistry High 38582451
2024 SAP102 forms subsynaptic nanoclusters that are smaller and denser than PSD-95 nanoclusters; only a subset of SAP102 nanoclusters co-organize with PSD-95, defining distinct MAGUK nanodomains within single synapses that differ in their enrichment of presynaptic Munc13-1. DNA-PAINT super-resolution microscopy; nanocluster analysis in rat cultured neurons The Journal of neuroscience Medium 38777601

Source papers

Stage 0 corpus · 58 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1996 SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo. Neuron 373 8780649
2008 Differential trafficking of AMPA and NMDA receptors by SAP102 and PSD-95 underlies synapse development. Proceedings of the National Academy of Sciences of the United States of America 184 19104036
1996 Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102. The Journal of biological chemistry 160 8702950
2004 Mutations in the DLG3 gene cause nonsyndromic X-linked mental retardation. American journal of human genetics 135 15185169
2006 Decreased NR1, NR2A, and SAP102 transcript expression in the hippocampus in bipolar disorder. Brain research 124 17113057
2001 Electron microscopic immunocytochemical detection of PSD-95, PSD-93, SAP-102, and SAP-97 at postsynaptic, presynaptic, and nonsynaptic sites of adult and neonatal rat visual cortex. Synapse (New York, N.Y.) 108 11309840
2005 mPins modulates PSD-95 and SAP102 trafficking and influences NMDA receptor surface expression. Nature cell biology 99 16299499
1997 Functional expression of rat synapse-associated proteins SAP97 and SAP102 in Drosophila dlg-1 mutants: effects on tumor suppression and synaptic bouton structure. Mechanisms of development 86 9152008
2010 Reduction in post-synaptic scaffolding PSD-95 and SAP-102 protein levels in the Alzheimer inferior temporal cortex is correlated with disease pathology. Journal of Alzheimer's disease : JAD 83 20634587
1999 Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD-95/SAP90. A possible regulatory role in molecular clustering at synaptic sites. The Journal of biological chemistry 79 10026200
2012 SAP102 mediates synaptic clearance of NMDA receptors. Cell reports 69 23103165
2003 Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 and SAP102. The Journal of biological chemistry 61 12576483
1997 Cloning and characterization of NE-dlg: a novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein. Oncogene 53 9188857
2011 NMDA receptor-dependent regulation of dendritic spine morphology by SAP102 splice variants. The Journal of neuroscience : the official journal of the Society for Neuroscience 49 21209193
2013 Postsynaptic density scaffold SAP102 regulates cortical synapse development through EphB and PAK signaling pathway. The Journal of neuroscience : the official journal of the Society for Neuroscience 48 23486974
2011 Dlg3 trafficking and apical tight junction formation is regulated by nedd4 and nedd4-2 e3 ubiquitin ligases. Developmental cell 46 21920314
2009 A novel mutation in the DLG3 gene encoding the synapse-associated protein 102 (SAP102) causes non-syndromic mental retardation. Neurogenetics 43 19795139
2020 Silence of lncRNA MIAT-mediated inhibition of DLG3 promoter methylation suppresses breast cancer progression via the Hippo signaling pathway. Cellular signalling 35 32593652
2014 Parallel mRNA and microRNA profiling of HEV71-infected human neuroblastoma cells reveal the up-regulation of miR-1246 in association with DLG3 repression. PloS one 32 24739954
1996 Isolation of a gene (DLG3) encoding a second member of the discs-large family on chromosome 17q12-q21. Genomics 31 8824795
2018 Tetrahedral DNA Nanomaterial Regulates the Biological Behaviors of Adipose-Derived Stem Cells via DNA Methylation on Dlg3. ACS applied materials & interfaces 25 30168311
2012 Synapse associated protein 102 (SAP102) binds the C-terminal part of the scaffolding protein neurobeachin. PloS one 25 22745750
1998 Immunocytochemical localization of the synapse-associated protein SAP102 in the rat retina. The Journal of comparative neurology 25 9674560
2000 NE-dlg, a mammalian homolog of Drosophila dlg tumor suppressor, induces growth suppression and impairment of cell adhesion: possible involvement of down-regulation of beta-catenin by NE-dlg expression. International journal of cancer 23 10797259
1999 A novel NE-dlg/SAP102-associated protein, p51-nedasin, related to the amidohydrolase superfamily, interferes with the association between NE-dlg/SAP102 and N-methyl-D-aspartate receptor. The Journal of biological chemistry 21 10542258
2015 Subunit-specific regulation of N-methyl-D-aspartate (NMDA) receptor trafficking by SAP102 protein splice variants. The Journal of biological chemistry 19 25555912
2020 LINC01315 Impairs microRNA-211-Dependent DLG3 Downregulation to Inhibit the Development of Oral Squamous Cell Carcinoma. Frontiers in oncology 17 33117688
2014 A two-state model for the diffusion of the A2A adenosine receptor in hippocampal neurons: agonist-induced switch to slow mobility is modified by synapse-associated protein 102 (SAP102). The Journal of biological chemistry 17 24509856
2024 The prediction of pCR and chemosensitivity for breast cancer patients using DLG3, RADL and Pathomics signatures based on machine learning and deep learning. Translational oncology 16 38805774
2019 High expression of DLG3 is associated with decreased survival from breast cancer. Clinical and experimental pharmacology & physiology 16 31271664
2024 DLG3 variants caused X-linked epilepsy with/without neurodevelopmental disorders and the genotype-phenotype correlation. Frontiers in molecular neuroscience 13 38249294
2017 Skewed X-inactivation in a family with DLG3-associated X-linked intellectual disability. American journal of medical genetics. Part A 13 28777483
2011 Fine mapping of Xq11.1-q21.33 and mutation screening of RPS6KA6, ZNF711, ACSL4, DLG3, and IL1RAPL2 for autism spectrum disorders (ASD). Autism research : official journal of the International Society for Autism Research 13 21384559
2024 Distinct SAP102 and PSD-95 Nano-organization Defines Multiple Types of Synaptic Scaffold Protein Domains at Single Synapses. The Journal of neuroscience : the official journal of the Society for Neuroscience 12 38777601
2017 Regulation of SAP102 Synaptic Targeting by Phosphorylation. Molecular neurobiology 12 29282697
2016 Altered thalamocortical development in the SAP102 knockout model of intellectual disability. Human molecular genetics 11 27466188
2011 Differential localization of SAP102 and PSD-95 is revealed in hippocampal spines using super-resolution light microscopy. Communicative & integrative biology 11 21509195
1998 DLG3, the gene encoding human neuroendocrine Dlg (NE-Dlg), is located within the 1.8-Mb dystonia-parkinsonism region at Xq13.1. Genomics 11 9598320
2018 Dynamic SAP102 expression in the hippocampal subregions of rats and APP/PS1 mice of various ages. Journal of anatomy 10 29574717
2018 SAP102 regulates synaptic AMPAR function through a CNIH-2-dependent mechanism. Journal of neurophysiology 10 30067114
2016 A non-coding variant in the 5' UTR of DLG3 attenuates protein translation to cause non-syndromic intellectual disability. European journal of human genetics : EJHG 10 27222290
2019 A Novel DLG3 Mutation Expanding the Phenotype of X-Linked Intellectual Disability Caused by DLG3 Nonsense Variants. Molecular syndromology 9 32021600
2012 Ligand binding of PDZ domains has various roles in the synaptic clustering of SAP102 and PSD-95. Neuroscience letters 9 23178474
1999 A recessive mutation leading to vertebral ankylosis in zebrafish is associated with amino acid alterations in the homologue of the human membrane-associated guanylate kinase DLG3. Mechanisms of development 9 10446262
2020 Triple diagnosis of Wiedemann-Steiner, Waardenburg and DLG3-related intellectual disability association found by WES: A case report. The journal of gene medicine 8 32246869
2021 Hypermethylation of DLG3 Promoter Upregulates RAC1 and Activates the PI3K/AKT Signaling Pathway to Promote Breast Cancer Progression. Evidence-based complementary and alternative medicine : eCAM 7 34765009
2024 Identification of a DLG3 stop mutation in the MRX20 family. European journal of human genetics : EJHG 3 38273165
2023 Distinct SAP102 and PSD-95 nano-organization defines multiple types of synaptic scaffold protein domains at single synapses. bioRxiv : the preprint server for biology 3 37745494
2023 COP1 facilitates the proliferation, invasion, and migration of glioma cells by ubiquitination of DLG3 protein. Neurological research 2 37356109
2011 Polymorphisms in the DLG3 gene is not associated with non-syndromic mental retardation in the Chinese Han population of Qin-Ba mountain. Cellular and molecular neurobiology 2 21369957
2008 Cloning and characterization of E-dlg, a novel splice variant of mouse homologue of the Drosophila discs large tumor suppressor binds preferentially to SAP102. IUBMB life 2 18618587
2025 A New Family with X-Linked Intellectual Disability 90: A Case Report of a Novel DLG3 Variant and Literature Review. Molecular syndromology 1 40881055
2025 Further phenotypical delineation of DLG3-related neurodevelopmental disorders. European journal of human genetics : EJHG 1 40983642
2024 JNK activity modulates postsynaptic scaffold protein SAP102 and kainate receptor dynamics in dendritic spines. The Journal of biological chemistry 1 38582451
2024 Multifaceted roles of DLG3/SAP102 in neurophysiology, neurological disorders and tumorigenesis. Neuroscience 1 39638232
2023 Sec8 specifically interacts with the PDZ2 domain of synapse associated protein 102 (SAP102). Frontiers in cell and developmental biology 1 37849738
2019 SAP102 contributes to hyperalgesia formation in the cancer induced bone pain rat model by anchoring NMDA receptors. Neuroscience letters 1 31682872
2024 Retraction: LINC01315 impairs microRNA-211-dependent DLG3 downregulation to inhibit the development of oral squamous cell carcinoma. Frontiers in oncology 0 39026977