Affinage

GRIP1

Glutamate receptor-interacting protein 1 · UniProt Q9Y3R0

Round 2 corrected
Length
1128 aa
Mass
122.4 kDa
Annotated
2026-04-28
108 papers in source corpus 44 papers cited in narrative 44 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

GRIP1 is a multi-domain scaffold protein that functions both as a transcriptional coregulator for nuclear receptors and inflammatory transcription factors and as a PDZ-domain adaptor orchestrating cargo transport and receptor trafficking in neurons. In the nucleus, GRIP1 uses LXXLL NR-box motifs and a unique repression domain to serve as a coactivator at palindromic GREs and as a corepressor at NF-κB and AP-1 tethering elements, with CDK9/CK2-mediated phosphorylation selectively potentiating its coactivator mode (PMID:8643509, PMID:11689447, PMID:22753499, PMID:29170386). In neurons, GRIP1 links AMPA receptor subunit GluA2, N-cadherin, and EphB2 to kinesin-1 motors for dendritic delivery, regulated by a phospho-Thr956/14-3-3 switch that controls kinesin attachment and by DHHC5/8-mediated palmitoylation that targets GRIP1 to recycling endosomes, and is required for LTP, homeostatic synaptic scaling, and learning and memory (PMID:11986669, PMID:24576423, PMID:22325201, PMID:32948689). Recessive loss-of-function mutations in GRIP1 cause Fraser syndrome in humans, linked to its essential role in localizing the basement-membrane protein Fras1 (PMID:22510445, PMID:14730302).

Mechanistic history

Synthesis pass · year-by-year structured walk · 21 steps
  1. 1996 High

    The initial identification of GRIP1 as a hormone-dependent interactor of steroid receptor hormone-binding domains established its founding role as a transcriptional coactivator bridging nuclear receptors to the basal transcription machinery.

    Evidence Yeast two-hybrid screen, in vitro binding, and mammalian reporter assays in mouse and mammalian cells

    PMID:8643509

    Open questions at the time
    • Mechanism of transcriptional activation undefined at the chromatin level
    • No information on in vivo physiological requirement
  2. 1998 High

    Mapping of three LXXLL NR-box motifs with receptor-specific preferences (NR Box II for ER, NR Box III for GR/AR) resolved how a single coactivator achieves selective interactions with diverse nuclear receptors.

    Evidence Site-directed mutagenesis combined with in vitro binding and mammalian two-hybrid/reporter assays

    PMID:9482670

    Open questions at the time
    • Structural basis of NR-box selectivity unknown
    • No auxiliary domain contribution yet mapped
  3. 1999 High

    Discovery of the AD2 domain as a docking site for CARM1 arginine methyltransferase showed that GRIP1 acts as a platform recruiting secondary coactivators whose enzymatic activities (histone methylation) are required for transcription.

    Evidence Co-immunoprecipitation, in vitro histone methylation assay, reporter assays with methyltransferase-dead CARM1 mutant

    PMID:10381882

    Open questions at the time
    • Chromatin substrate specificity of GRIP1-recruited CARM1 in vivo not defined
    • Relationship to other histone-modifying enzymes unclear
  4. 2001 High

    The demonstration that GRIP1 functions as a GR corepressor at AP-1 tethering GREs, using domains overlapping with but functionally distinct from its coactivator surfaces, overturned the view that p160 family members serve exclusively as coactivators.

    Evidence ChIP at the native collagenase-3 gene, reporter assays with deletion mutants, dominant-negative experiments

    PMID:11689447

    Open questions at the time
    • Identity of cofactors mediating the intrinsic repression activity unknown
    • Genome-wide scope of corepression not yet mapped
  5. 2002 High

    Identification of a GRIP1-specific repression domain absent from SRC1/RAC3, combined with demonstration of context-dependent repression mechanisms at AP-1 vs. NF-κB vs. osteocalcin GREs, established that GRIP1 uses structurally separable surfaces for coactivation and corepression at different genomic loci.

    Evidence Systematic Gal4-fusion domain mapping with multiple reporter constructs and response elements

    PMID:12481024

    Open questions at the time
    • Direct binding partners of the repression domain not identified
    • No structural information on the repression domain
  6. 2002 High

    The finding that GRIP1 directly binds kinesin heavy chains (KIF5) and steers kinesin-dependent transport specifically to dendrites provided the first evidence for GRIP1 as a motor adaptor outside the nucleus, explaining its somatodendritic localization.

    Evidence Yeast two-hybrid, co-immunoprecipitation, KIF5 knockout mice, dominant-negative kinesin-binding domain overexpression

    PMID:11986669

    Open questions at the time
    • Cargo identity of GRIP1-kinesin complexes not fully resolved
    • Regulatory mechanism controlling kinesin attachment unknown
  7. 2002 High

    Crystal structures of the PDZ6 domain alone and in complex with liprin-α1 peptide, and later the PDZ12 supramodule with Fras1 peptide, provided atomic-level understanding of GRIP1 cargo recognition and revealed that PDZ1 folding strictly requires PDZ2 as an obligate partner.

    Evidence X-ray crystallography at 1.5–1.8 Å resolution with in vitro binding validation

    PMID:12493751 PMID:18155042

    Open questions at the time
    • Structures of PDZ4-6 in complex with GluA2 not available
    • Full-length GRIP1 architecture unresolved
  8. 2002 High

    Genetic knockout studies showed GRIP1 is essential for viability and tissue integrity: complete KO caused embryonic lethal epidermolysis bullosa-like blistering, while a viable null showed impaired fertility from defective Sertoli cell-germ cell adhesion and placental hypoplasia, establishing in vivo requirements beyond transcription.

    Evidence Two independent GRIP1 KO mouse lines with histological, ultrastructural, and fertility phenotyping

    PMID:11983858 PMID:12138202

    Open questions at the time
    • Molecular mechanism linking GRIP1 to dermo-epidermal junction assembly not elucidated
    • Cell-type contributions to embryonic lethality unclear
  9. 2004 High

    The discovery that GRIP1 physically interacts with the ECM protein Fras1 and is required for its basal membrane localization, with GRIP1 loss phenocopying Fraser syndrome in mice, connected GRIP1's scaffolding function to a specific developmental pathway.

    Evidence Co-immunoprecipitation, immunofluorescence, genetic mouse models (GRIP1 KO and eye-blebs mouse)

    PMID:14730302

    Open questions at the time
    • How GRIP1 delivers Fras1 to the basement membrane mechanistically unresolved
    • Whether other FRAS1/FREM complex members require GRIP1 not tested
  10. 2005 High

    GRIP1 was shown to control dendrite morphogenesis by linking EphB2 receptors to KIF5-powered dendritic transport; GRIP1 knockdown caused dendrite loss that was rescued by EphB2 extracellular domain, causally connecting GRIP1-kinesin trafficking to dendritic growth signaling.

    Evidence RNAi knockdown, rescue experiments, dominant-negative EphB2, EphB triple-KO neurons

    PMID:15965473

    Open questions at the time
    • Upstream signals initiating GRIP1-EphB2 loading onto kinesin unknown
    • Role in axonal vs. dendritic specification of transport unclear
  11. 2005 High

    Identification of IRF3 as a direct binding partner of the GRIP1 repression domain in macrophages, with GR and IRF3 competing for GRIP1, revealed that GRIP1 integrates innate immune and glucocorticoid signaling through a shared surface.

    Evidence Yeast two-hybrid, co-immunoprecipitation, siRNA, macrophage gene expression, MyD88/IFNAR-deficient mice

    PMID:16362036

    Open questions at the time
    • Stoichiometry of GR-GRIP1-IRF3 competition in vivo not quantified
    • Genome-wide targets of GRIP1-IRF3 pathway uncharacterized
  12. 2010 High

    Conditional GRIP1/2 double knockout in neurons demonstrated that GRIP proteins are dispensable for steady-state AMPAR trafficking but essential for activity-dependent AMPAR recycling, mediated through direct interaction with the exocyst complex.

    Evidence Neuron-specific conditional KO, co-immunoprecipitation with exocyst, electrophysiology, live imaging

    PMID:20956289

    Open questions at the time
    • Which exocyst subunit directly contacts GRIP1 undefined
    • Mechanism of exocyst activation by GRIP1 unknown
  13. 2012 High

    DHHC5/8-mediated palmitoylation of GRIP1b was found to target it to trafficking endosomes and accelerate AMPAR recycling, establishing a lipid modification as a key regulatory switch for GRIP1's transport adaptor function.

    Evidence ABE palmitoylation chemistry, live imaging of endosomal targeting, AMPAR recycling assays

    PMID:22325201

    Open questions at the time
    • Depalmitoylation enzyme not identified
    • Relationship between palmitoylation and phospho-Thr956 regulation not tested
  14. 2012 High

    Conditional hematopoietic GRIP1 deletion proved that GRIP1 is recruited to NF-κB sites with GR in macrophages and is required for glucocorticoid-mediated anti-inflammatory repression in vivo, with GRIP1-deficient mice showing sensitization to LPS-induced shock.

    Evidence Hematopoietic-specific conditional KO, ChIP, genome-wide transcriptomics, in vivo LPS challenge

    PMID:22753499

    Open questions at the time
    • GRIP1 repression domain cofactors at NF-κB sites not identified
    • Therapeutic relevance of dissociating GRIP1 coactivator from corepressor activity unexplored
  15. 2012 High

    Human recessive GRIP1 mutations were identified as a cause of Fraser syndrome, validating the mouse phenotype and establishing GRIP1 as a disease gene for this congenital disorder.

    Evidence Linkage analysis and Sanger sequencing in multiple families, RT-PCR splice-site characterization

    PMID:22510445

    Open questions at the time
    • Genotype-phenotype correlation across GRIP1 mutation spectrum not explored
    • Whether partial loss-of-function causes milder phenotypes unknown
  16. 2014 High

    Discovery that phosphorylation of GRIP1 at Thr956 creates a 14-3-3 binding site that detaches GRIP1 from kinesin-1 revealed a regulatory switch for cargo transport, and T956A knock-in mice displayed impaired dendrite morphogenesis, directly linking this phospho-switch to neuronal development.

    Evidence Phospho-dependent binding assays, co-immunoprecipitation, T956A transgenic mice with dendrite morphology analysis

    PMID:24576423

    Open questions at the time
    • Kinase responsible for Thr956 phosphorylation in neurons not definitively established in this study
    • 14-3-3 isoform specificity not determined
  17. 2015 High

    GRIP1 was shown to be essential for homeostatic synaptic scaling: its synaptic abundance increases with activity deprivation, and GRIP1 loss blocks scaling-up of AMPAR-mediated currents, with the GRIP1-GluA2 interaction specifically required for the plasticity readout.

    Evidence Conditional KO neurons, shRNA knockdown-replace with interaction mutants, electrophysiology (mEPSC recordings)

    PMID:26109571 PMID:26216979

    Open questions at the time
    • Signal transduction pathway from inactivity sensing to GRIP1 synaptic accumulation unknown
    • Whether GRIP1 acts pre- or post-endosomally in scaling not resolved
  18. 2017 High

    CDK9 was identified as the kinase phosphorylating GRIP1's N-terminal serine cluster within GR:GRIP1:CDK9 complexes, and genome-wide ChIP-seq revealed phospho-GRIP1 selectively occupies GRE coactivation sites but is absent from corepression sites, mechanistically separating the two opposing functions.

    Evidence Kinase assays, phospho-specific antibodies, ChIP-seq, macrophage conditional KO models

    PMID:29170386

    Open questions at the time
    • CK2 contribution to individual phospho-sites not fully resolved
    • Phosphatase counteracting GRIP1 phosphorylation unknown
  19. 2017 High

    GRIP1 was found to scaffold a multi-receptor complex containing ApoER2, ephrinB2, and AMPARs via PDZ domains; phosphorylation of ephrinB2 at Ser-9 stabilizes this complex, and its disruption in knock-in mice abolishes activity-induced AMPAR insertion and LTP.

    Evidence Co-immunoprecipitation, PDZ binding assays, ephrinB2-S9A knock-in mice, electrophysiology (LTP)

    PMID:28978486

    Open questions at the time
    • Kinase phosphorylating ephrinB2 Ser-9 not identified
    • Structural basis of the quaternary complex not determined
  20. 2020 High

    Conditional neuronal GRIP1 knockout demonstrated its requirement for hippocampal LTP and spatial learning/memory, with GluA2-Y876 phosphorylation enhancing GRIP1-AMPAR binding during LTP while GluA2-S880 phosphorylation decreases, providing a molecular code for activity-dependent GRIP1 engagement.

    Evidence Conditional neuronal KO, hippocampal slice electrophysiology, behavioral memory testing, phospho-specific immunoblots during glycine-LTP

    PMID:32948689

    Open questions at the time
    • Kinase responsible for GluA2-Y876 phosphorylation during LTP not confirmed in GRIP1 KO context
    • Circuit-level specificity of GRIP1 requirement across hippocampal subregions not mapped
  21. 2025 High

    A gain-of-function GRIP1 variant (I507L) with increased GluA2 binding selectively abolished homeostatic scaling-up without affecting Hebbian LTP, dissociating the two plasticity modes mechanistically through the GluA2-Y876 phosphorylation pathway and linking GRIP1-AMPAR interaction strength to autism-like behavioral phenotypes.

    Evidence Knock-in mouse model, behavioral testing, electrophysiology, phospho-specific immunoblots

    PMID:41390787

    Open questions at the time
    • Whether gain-of-function variants exist in human ASD populations unknown
    • Cell-type specificity of scaling deficit not resolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How GRIP1's nuclear coregulatory and cytoplasmic cargo-adaptor functions are coordinated within the same cell, and what governs the partitioning of GRIP1 between these compartments, remains mechanistically unresolved.
  • Full-length GRIP1 structure unavailable
  • No integrated model connecting nuclear and cytoplasmic GRIP1 pools
  • Depalmitoylation enzyme and phosphatases opposing GRIP1 regulatory switches not identified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140110 transcription regulator activity 10 GO:0060090 molecular adaptor activity 7
Localization
GO:0005634 nucleus 6 GO:0005829 cytosol 3 GO:0005856 cytoskeleton 2 GO:0005886 plasma membrane 2 GO:0031410 cytoplasmic vesicle 2
Pathway
R-HSA-112316 Neuronal System 7 R-HSA-74160 Gene expression (Transcription) 7 R-HSA-1266738 Developmental Biology 3 R-HSA-162582 Signal Transduction 3 R-HSA-168256 Immune System 3
Partners
CARM1CDK9CTNNB1EPHB2FRAS1GLUR2KIF5CNR3C1
Complex memberships
ApoER2-ephrinB2-GRIP1-AMPAR complexGR:GRIP1:CDK9 complexGRIP1-KIF5 transport complex

Evidence

Reading pass · 44 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1996 GRIP1 (glucocorticoid receptor-interacting protein 1) was identified as a novel mouse protein that interacts with the hormone-binding domains (HBDs) of glucocorticoid, estrogen, and androgen receptors in a hormone-regulated manner, and functions as a transcriptional coactivator by bridging steroid receptor HBDs to the basal transcription machinery in yeast and mammalian cells. Yeast two-hybrid screen, in vitro interaction assays, mammalian reporter gene assays, squelching assays Proceedings of the National Academy of Sciences of the United States of America High 8643509
1997 Full-length GRIP1 (1,462 aa) is the mouse ortholog of human TIF2, interacts in a hormone-dependent manner with HBDs of all five steroid receptors and class II nuclear receptors (TR, VDR, RAR, RXR), and acts as a coactivator specifically for the AF-2 (but not AF-1) transactivation domain of the glucocorticoid receptor. Yeast two-hybrid, in vitro binding, mammalian transient transfection reporter assays, GR truncation and point mutant analysis Molecular and cellular biology High 9111344
1998 GRIP1 contains three LXXLL NR box motifs (NR Box I, II, III) in its central region; NR Box II and III are crucial for functional and binding interactions with nuclear receptors. Different nuclear receptors show distinct NR Box preferences: estrogen receptor interactions depend more on NR Box II, while androgen receptor and glucocorticoid receptor interactions depend more on NR Box III. Site-directed mutagenesis of NR box motifs, in vitro binding assays, mammalian two-hybrid and reporter assays Molecular endocrinology High 9482670
1998 GRIP1 associates with hepatocyte nuclear factor 4 (HNF4) in vivo and enhances HNF4 transactivation; the AF-2 domain of HNF4 is required for both interaction and coactivation. GRIP1 also synergizes with p300 to further enhance HNF4 activity, and drives expression from the HNF1 gene promoter through an intact HNF4-binding site. Co-immunoprecipitation, mammalian reporter gene assays, promoter deletion analysis The Journal of biological chemistry Medium 9812974
1999 GRIP1 contains an auxiliary nuclear receptor interaction domain (NIDaux, aa 1011–1121) in addition to its central NID; both domains must act in cis for efficient interaction with a subset of nuclear receptors including GR, AR, and RARα. The NIDaux region also harbors a separable p300-interaction domain. Deletion mapping, in vitro binding assays, mammalian two-hybrid assays, mutagenesis The Journal of biological chemistry High 9920895
1999 CARM1 (coactivator-associated arginine methyltransferase 1) binds to the C-terminal AD2 domain of GRIP1 and functions as a secondary coactivator for nuclear receptors, enhancing transcriptional activation only when GRIP1 is coexpressed; CARM1 methylates histone H3 in vitro and this methyltransferase activity is required for its coactivator function. Co-immunoprecipitation, in vitro methylation assay, mammalian reporter gene assays, domain mapping, mutagenesis of SAM-binding domain Science High 10381882
2001 GRIP1 (TIF2) acts as a GR corepressor at the collagenase-3 gene AP-1 tethering GRE: it is recruited to the col3A response element through protein-protein interactions with DNA-bound AP-1, and potentiates GR-mediated repression in an agonist-dependent but not antagonist-dependent manner. GRIP1 mutants deficient in GR binding and coactivator functions are also defective for corepression. Chromatin immunoprecipitation, mammalian reporter assays, GRIP1 mutant analysis, dominant-negative experiments The EMBO journal High 11689447
2001 GRIP1 localizes in discrete nuclear foci dependent on its C-terminal activation domains (AD1 and AD2); a subpopulation of foci associates with ND10/PML nuclear bodies through the AD1 (CBP-interacting) domain; GRIP1 foci are enriched in 26S proteasome components and GRIP1 is degraded by the proteasome, as demonstrated by increased fluorescence intensity upon proteasome inhibitor treatment. GFP-fusion live-cell imaging, deletion mutant analysis, proteasome inhibitor treatment (lactacystin), fluorescence microscopy Molecular endocrinology Medium 11266502
2002 GRIP1 directly interacts with kinesin heavy chains (KIF5) and steers kinesin-dependent transport to dendrites. Gene targeting and dominant-negative experiments of kinesin heavy chains showed abnormal GRIP1 localization; expression of the kinesin-binding domain of GRIP1 caused accumulation of endogenous kinesin in the somatodendritic area, distinct from the somatoaxonal distribution caused by the kinesin-binding scaffold JSAP1. Yeast two-hybrid, co-immunoprecipitation, gene targeting (KO mice), dominant-negative overexpression, immunofluorescence localization Nature High 11986669
2002 GRIP1 functions in two distinct modes of GR-mediated repression using different surfaces: at AP-1 tethering GREs (collagenase-3) and NF-κB tethering GREs (IL-8), a specific GRIP1 repression domain (distinct from AD1 and AD2 activation domains) is required; this domain has intrinsic GR-independent repression activity and is absent from other p160 family members SRC1 and RAC3. At osteocalcin GREs, repression uses a different mechanism not requiring this GRIP1-specific domain. Mammalian reporter gene assays with deletion mutants, Gal4-fusion domain mapping, response element comparison across gene contexts Proceedings of the National Academy of Sciences of the United States of America High 12481024
2002 The nuclear receptor interaction domain of GRIP1 is modulated by SUMO-1 modification at lysines 239, 731, and 788; Lys-731 and Lys-788 (located in the NID) are principal SUMO-1 attachment sites, and their mutation impairs GRIP1 colocalization with androgen receptor in nuclei and attenuates AR-dependent transcription and synergy with PIASxβ. Site-directed mutagenesis, sumoylation assays, confocal microscopy colocalization, mammalian reporter gene assays The Journal of biological chemistry High 12060666
2002 Loss of murine GRIP1 causes embryonic lethality with epidermolysis bullosa-like skin blistering (below the lamina densa) at E12, indicating that GRIP1 scaffolding is required for formation and integrity of the dermo-epidermal junction. Genetic knockout (GRIP1-/- mice), histology, electron microscopy Proceedings of the National Academy of Sciences of the United States of America High 11983858
2002 The crystal structure of GRIP1 PDZ6 domain alone and in complex with the C-terminal octapeptide of liprin-α1 was determined at 1.5 Å and 1.8 Å resolution, revealing that Ile-736 (not the conserved Leu-732) makes the critical hydrophobic contact with the -2 position Tyr of the ligand, and that PDZ6 forms an antiparallel dimer through a site distal to the peptide-binding groove, enabling GRIP1 multimerization. X-ray crystallography (1.5 Å and 1.8 Å resolution structures) The Journal of biological chemistry High 12493751
2002 Antiandrogens (hydroxyflutamide, bicalutamide) block agonist-activated AR from recruiting GRIP1 to colocalize in nuclei, whereas the mixed antagonist/agonist cyproterone acetate promotes AR-GRIP1 colocalization and transcriptional activation, demonstrating that ligand-dependent GRIP1 recruitment correlates with AR transcriptional activity. Confocal microscopy colocalization of AR and GRIP1-GFP, reporter gene assays FEBS letters Medium 12123801
2002 The TIF2/GRIP1 knockout mouse is viable (unlike a previous partial-KO that was embryonic lethal) but shows impaired fertility in both sexes: male hypofertility is due to teratozoospermia and age-dependent testicular degeneration with defective Sertoli cell-germ cell adhesion; female hypofertility is due to placental hypoplasia in decidua stromal cells. Conditional/conventional gene targeting (TIF2-/- mice), histological and morphological phenotyping, fertility testing Molecular and cellular biology High 12138202
2003 GRIP1 and β-catenin interact directly through the AD2 domain of GRIP1, and synergistically enhance transcription driven by both androgen receptor (AR) and Lef1. While GRIP1 directly binds AR, its coactivation of Lef1 is entirely dependent on β-catenin as a bridge, representing a novel indirect coactivator recruitment mechanism. Co-immunoprecipitation, mammalian reporter gene assays, chromatin immunoprecipitation, domain mapping The Journal of biological chemistry Medium 14638683
2004 GRIP1 physically interacts with Fras1 (a basement membrane ECM protein) and is required for the localization of Fras1 to the basal side of cells. Loss of Grip1 (by a two-exon deletion in the eye-blebs mouse) causes Fraser syndrome-like defects (subepidermal blistering, renal agenesis, syndactyly, cryptophthalmos), phenocopying Fras1 mutations. Co-immunoprecipitation, immunofluorescence localization, genetic mouse models (GRIP1 KO and eb mouse), phenotypic analysis Nature genetics High 14730302
2004 cAMP-dependent protein kinase (PKA) induces ubiquitination and proteasomal degradation of GRIP1, reducing its half-life. PKA activation stimulates GRIP1 recruitment to subnuclear foci colocalized with the proteasome. This is confirmed by ubiquitin-E1 temperature-sensitive cell lines and proteasome inhibitors. Pulse-chase experiments, proteasome inhibitor treatment, temperature-sensitive E1 cell lines, co-immunoprecipitation for ubiquitination, GFP-GRIP1 live imaging The Journal of biological chemistry High 15347661
2004 GRIP1 acts as a corepressor (not coactivator) for MyoD-mediated transcription, while SRC1A and p/CIP act as coactivators; GRIP1 binds both the N-terminal activation domain regions of MyoD used by SRC1A and p/CIP, and also uniquely interacts with MyoD sites critical for p300 binding, suggesting competitive inhibition of coactivator assembly. Mammalian reporter gene assays, domain-specific pulldowns and binding assays, mutagenesis The Journal of biological chemistry Medium 15563453
2005 GRIP1 knockdown by siRNA in hippocampal neurons causes loss of dendrites, associated with mislocalization of GluR2, EphB2, and KIF5. The dendritic loss is rescued by overexpression of the extracellular domain of EphB2 and phenocopied by dominant-negative EphB2 or ephrinB-Fc. Disruption of the KIF5-GRIP1 interaction specifically inhibits EphB2 trafficking and impairs dendritic growth. RNAi knockdown, rescue experiments, dominant-negative overexpression, EphB1/2/3 triple KO neurons, immunofluorescence localization Nature neuroscience High 15965473
2005 GRIP1 interacts with the GABA-A receptor-associated protein GABARAP directly through PDZ domains 4-6, and this interaction is confirmed in vivo by co-immunoprecipitation; GRIP1 colocalizes with γ2 subunit-containing GABA-A receptors in hippocampal neurons, suggesting a role at inhibitory synapses. In vitro protein interaction assays (GST pulldown), co-immunoprecipitation, immunofluorescence colocalization Biochemical pharmacology Medium 15451408
2005 The GRIP1 corepression domain directly interacts with IRF3 (interferon regulatory factor 3), a downstream effector of TLR3/4. Endogenous GRIP1 and IRF3 interact in macrophages; GR activation or GRIP1 knockdown blocks IRF3-dependent gene expression, while GRIP1 overexpression rescues it. GR and IRF3 compete for GRIP1 binding. Yeast two-hybrid, co-immunoprecipitation, GRIP1 siRNA knockdown, macrophage reporter and gene expression assays, MyD88/IFNAR-deficient mouse experiments The EMBO journal High 16362036
2005 GRIP1 mediates the interaction between the androgen receptor N-terminal domain (AR-NTD) and C-terminal ligand-binding domain (AR-LBD) by simultaneously binding both domains; mutation abolishing N/C interaction can be rescued by wild-type GRIP1 but not by GRIP1 mutants lacking either AR interaction domain. Mammalian two-hybrid, co-immunoprecipitation, mutagenesis of AR and GRIP1 Biological chemistry Medium 15843149
2007 The crystal structure of GRIP1 PDZ12 tandem in complex with the Fras1 C-terminal peptide reveals that PDZ1 and PDZ2 form a supramodule (PDZ1 folding strictly requires PDZ2 attachment); only PDZ1's peptide-binding groove engages the Fras1 peptide, explaining the molecular basis of GRIP1-Fras1 interaction and its link to Fraser syndrome. X-ray crystallography, in vitro binding assays, deletion analysis Journal of molecular biology High 18155042
2007 GRIP1 acts as a platform molecule mediating differential RA-induced coregulator recruitment to the TR2/IR0 promoter: in undifferentiated preadipocytes GRIP1 recruits PCAF (histone acetyltransferase complex) to activate TR2, while in differentiated adipocytes it recruits RIP140 (histone deacetylase-containing complex) to repress TR2. GRIP1 directly interacts with RIP140 through its AD2 domain. Chromatin immunoprecipitation, co-immunoprecipitation, reporter assays, siRNA knockdown Nucleic acids research Medium 17389641
2010 GRIP1 and GRIP2 regulate activity-dependent AMPA receptor recycling via direct interactions with the exocyst protein complex; GRIP1/2 double KO impairs activity-dependent AMPAR recycling without affecting steady-state trafficking or endocytosis, and disruption of GRIP1-exocyst binding causes a similar recycling deficit. Conditional KO (neuron-specific GRIP1 KO in GRIP2 KO background), co-immunoprecipitation with exocyst complex, electrophysiology, live imaging Proceedings of the National Academy of Sciences of the United States of America High 20956289
2011 Endogenous GRIP1 undergoes glucocorticoid-induced, GR-interaction-dependent phosphorylation at one constitutive and six inducible sites; CDK9 and CK2 are identified as putative GRIP1 kinases. Phospho-specific GRIP1 isoforms are recruited in a response element-specific manner to native GR targets, and phosphorylation is functionally required for GR-activated transcription. Mass spectrometry phosphoproteomics, phospho-specific antibodies, mutagenesis, ChIP, mammalian reporter assays Molecular and cellular biology High 22158970
2012 GRIP1b is specifically palmitoylated by DHHC5 and DHHC8 palmitoyl acyltransferases; this interaction requires a PDZ ligand unique to DHHC5/8. Palmitoylated GRIP1b is targeted to trafficking endosomes, links endosomes to kinesin motors, and palmitoylation accelerates AMPA receptor recycling. GRIP1b has one of the highest palmitoylation turnover rates reported. Binding assays, palmitoylation assays (ABE chemistry), live imaging of endosomal targeting, AMPAR recycling assays, turnover measurements Neuron High 22325201
2012 GRIP1 acts as a GR corepressor in primary macrophages, recruited to p65-occupied NFκB-binding sites in conjunction with liganded GR. Conditional hematopoietic cell-specific GRIP1 deletion attenuates GR-mediated repression of NFκB target genes in a dose-dependent manner, and GRIP1-deficient mice are sensitized to LPS-induced shock. Conditional KO (hematopoietic-specific GRIP1 deletion), ChIP, genome-wide transcriptomics, in vivo LPS challenge Proceedings of the National Academy of Sciences of the United States of America High 22753499
2012 Recessive mutations in human GRIP1 (splice-site mutation causing exon 17 skipping and frameshift, and a 4-bp deletion) cause classic Fraser syndrome, demonstrating GRIP1's essential role in human embryonic development. Genetic linkage analysis, Sanger sequencing, RT-PCR characterization of splice mutation in patient samples Journal of medical genetics High 22510445
2014 GRIP1 interlinks N-cadherin and GluA2-containing AMPARs at the same transport vesicles via different PDZ domains (PDZ2 for N-cadherin, PDZ4-6 for GluA2) for combined KIF5-powered dendritic delivery; interference with either binding motif impairs turnover of both synaptic cargoes, and co-transport is confirmed by live imaging. Co-immunoprecipitation, live imaging of cotransport, domain deletion analysis, microtubule depolymerization, electrophysiology, spine counting Proceedings of the National Academy of Sciences of the United States of America High 24639525
2014 GRIP1 interacts with 14-3-3 proteins in a phospho-dependent manner at Thr956; 14-3-3 binds the kinesin-1-binding region of GRIP1, detaching GRIP1 from kinesin-1 and thereby regulating cargo transport. A T956A point mutation in transgenic mice impairs dendritic development, demonstrating that phosphorylation-regulated kinesin attachment is essential for dendrite morphogenesis. Co-immunoprecipitation, phospho-dependent binding assays, transgenic point-mutant mice (T956A), dendrite morphology analysis Developmental cell High 24576423
2015 GRIP1 expression is bidirectionally regulated by neuronal activity; GRIP1 redistributes subcellularly and changes its binding to GluA2 during synaptic scaling. GRIP1 loss blocks surface AMPAR accumulation and scaling-up of synaptic strength following chronic activity blockade, demonstrating an essential role in homeostatic AMPAR trafficking. Biochemical fractionation, co-immunoprecipitation, conditional KO neurons, electrophysiology (mEPSC recordings), live imaging Proceedings of the National Academy of Sciences of the United States of America High 26216979
2015 Synaptic abundance of GRIP1 is enhanced by activity deprivation; direct overexpression of GRIP1 increases AMPA mEPSC amplitude, and shRNA-mediated GRIP1 knockdown prevents scaling-up. Knockdown-replace experiments show that scaling-up requires the GRIP1-GluA2 interaction; GRIP1 synaptic accumulation during scaling-up does not require GluA2 binding. shRNA knockdown, overexpression, knockdown-replace with interaction-mutant GRIP1 and GluA2, electrophysiology Proceedings of the National Academy of Sciences of the United States of America High 26109571
2015 Trip6 interacts with GRIP1 and myosin VI to promote dendritic morphogenesis. Phosphorylation of GRIP1 at Thr956 by AKT1 inhibits GRIP1-myosin VI interaction and facilitates GRIP1 binding to 14-3-3, which regulates F-actin organization and dendritic morphogenesis. Co-immunoprecipitation, siRNA knockdown, phosphorylation assays, F-actin measurements, dendritic morphology analysis The Journal of neuroscience Medium 25673849
2016 GRIP1 facilitates macrophage alternative (M2) programming via a GR-independent pathway by serving as a coactivator for KLF4, a driver of tissue-resident macrophage differentiation. Conditional GRIP1 deletion in macrophages in obese mice causes massive macrophage infiltration, fatty livers, hyperglycemia, and insulin resistance. Conditional macrophage-specific GRIP1 KO, chromatin immunoprecipitation, reporter assays, in vivo metabolic phenotyping Nature communications High 27464507
2017 GRIP1 is phosphorylated at an N-terminal serine cluster by CDK9, which is recruited into GC-induced GR:GRIP1:CDK9 hetero-complexes. Phosphorylation potentiates GRIP1 coactivator function at palindromic GRE sites but not its corepressor properties at pro-inflammatory gene transrepression sites, and phospho-GRIP1 is absent from GR transrepression sites. Co-immunoprecipitation, kinase assays, phospho-specific antibodies, ChIP-seq, genome-wide binding analysis, macrophage KO models Nature communications High 29170386
2017 GRIP1 binds ApoER2 via PDZ domains and bridges a complex containing ApoER2, ephrinB2, and AMPA receptors. Phosphorylation of ephrinB2 at Ser-9 is required for complex stability; mutation of ephrinB2 Ser-9 in mice disrupts this complex, abolishes ApoER2 downstream signaling, and impairs activity-induced AMPAR insertion and LTP. Co-immunoprecipitation, PDZ domain binding assays, knock-in mouse (ephrinB2-S9A), electrophysiology (LTP), compound genetic experiments Cell reports High 28978486
2019 HAP1a and GRIP1 form a protein complex in the brain and cooperate to activate kinesin-1 subunit KIF5C in vitro; this cooperative activation involves stabilization of the central hinge region critical to kinesin-1 autoinhibition. Co-immunoprecipitation from brain lysates, in vitro kinesin activation assay Journal of cell science Medium 31757889
2019 Purkinje cell-specific Grip1/2 knockout mice show increased repetitive self-grooming and impaired mGluR-LTD at parallel fiber-PC synapses, with increased mGluR5 and Arc expression and enhanced phosphorylation of P38 and AKT in cerebellum, linking GRIP1/2-mediated AMPAR trafficking in PCs to repetitive behavior. Conditional KO (L7-Cre driven Grip1/2 KO), behavioral testing, electrophysiology (mEPSCs, mGluR-LTD), immunoblots Neurobiology of disease High 31476380
2020 GRIP1 is required for LTP and learning and memory; GRIP1 is recruited into synapses during LTP, and Grip1 KO mice show impaired hippocampal LTP and memory deficits. During chemically induced LTP, GluA2-S880 phosphorylation decreases while GluA2-Y876 phosphorylation increases, enhancing the GRIP1-AMPAR association and promoting AMPAR insertion into the postsynaptic membrane. Conditional neuronal KO, electrophysiology (LTP in hippocampal slices), behavioral testing (memory), biochemical phosphorylation analysis, glycine-LTP protocol Proceedings of the National Academy of Sciences of the United States of America High 32948689
2021 EphrinB2 and GRIP1 cooperate to stabilize mushroom spines and mediate AMPAR relocation to mushroom spine surfaces during homeostatic plasticity following denervation; EphB4 stimulation prevents lesion-induced mushroom spine loss and rescues spine recovery in a GRIP1 dominant-negative background. Repetitive live imaging, expansion microscopy, dominant-negative GRIP1 expression, EphB4 stimulation, quantitative AMPAR surface/intracellular pool analysis Cell reports Medium 33789115
2024 GRIP1 associates with vimentin filaments in endothelial cells and co-immunoprecipitates with vimentin; GRIP1 knockout in human endothelial cells causes loss of focal adhesions and altered adhesive properties, suggesting GRIP1 mediates kinesin-1-dependent delivery of vimentin filaments to the cell periphery to contact and stabilize focal adhesions. Co-immunoprecipitation, GRIP1 gene KO in endothelial cells, immunofluorescence of focal adhesions Molekuliarnaia biologiia Low 39970118
2025 A gain-of-function GRIP1 variant (I507L in mice) shows increased binding to GluA2, and Grip1-I507L mice exhibit impaired social interaction, increased repetitive behaviors, increased neuronal excitability, and loss of synaptic upscaling to inactivity. Basal GluA2-Y876 phosphorylation is elevated and cannot be further induced by inactivity, mechanistically explaining loss of homeostatic scaling without affecting GluA2-S880-dependent Hebbian plasticity. Knock-in mouse model, behavioral testing, electrophysiology, co-immunoprecipitation, phospho-specific immunoblots Molecular psychiatry High 41390787

Source papers

Stage 0 corpus · 108 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2861 17081983
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
1997 The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 1099 9192892
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
1999 Regulation of transcription by a protein methyltransferase. Science (New York, N.Y.) 991 10381882
1996 TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. The EMBO journal 904 8670870
2018 VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop codon and associates with alternative polyadenylation. Cell discovery 829 29507755
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2002 Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell 670 12151000
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
1996 GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. Proceedings of the National Academy of Sciences of the United States of America 598 8643509
2018 High-Density Proximity Mapping Reveals the Subcellular Organization of mRNA-Associated Granules and Bodies. Molecular cell 580 29395067
1999 Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell 543 10490106
1997 GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Molecular and cellular biology 482 9111344
2015 A Dynamic Protein Interaction Landscape of the Human Centrosome-Cilium Interface. Cell 433 26638075
2022 OpenCell: Endogenous tagging for the cartography of human cellular organization. Science (New York, N.Y.) 432 35271311
1998 The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. The EMBO journal 430 9430642
1998 Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature 420 9590696
2005 Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. Genome research 409 16344560
2002 Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites. Nature 397 11986669
1998 Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): multiple motifs with different binding specificities. Molecular endocrinology (Baltimore, Md.) 367 9482670
2021 A proximity-dependent biotinylation map of a human cell. Nature 339 34079125
2000 Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Molecular and cellular biology 325 10594042
2001 Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities. The Journal of biological chemistry 297 11050077
2017 Genome-wide CRISPR screen identifies HNRNPL as a prostate cancer dependency regulating RNA splicing. Proceedings of the National Academy of Sciences of the United States of America 282 28611215
2002 T0070907, a selective ligand for peroxisome proliferator-activated receptor gamma, functions as an antagonist of biochemical and cellular activities. The Journal of biological chemistry 276 11877444
2004 Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. Nature biotechnology 266 15146197
2011 Identification of a novel, recurrent HEY1-NCOA2 fusion in mesenchymal chondrosarcoma based on a genome-wide screen of exon-level expression data. Genes, chromosomes & cancer 244 22034177
2014 Genetic association study of QT interval highlights role for calcium signaling pathways in myocardial repolarization. Nature genetics 243 24952745
2002 Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator activity by I kappa B kinase. Molecular and cellular biology 226 11971985
1998 A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia. Blood 220 9558366
2014 Proximity biotinylation and affinity purification are complementary approaches for the interactome mapping of chromatin-associated protein complexes. Journal of proteomics 215 25281560
2002 The function of TIF2/GRIP1 in mouse reproduction is distinct from those of SRC-1 and p/CIP. Molecular and cellular biology 210 12138202
1999 Characterization of the glutamate receptor-interacting proteins GRIP1 and GRIP2. The Journal of neuroscience : the official journal of the Society for Neuroscience 195 10436050
2002 Alternate surfaces of transcriptional coregulator GRIP1 function in different glucocorticoid receptor activation and repression contexts. Proceedings of the National Academy of Sciences of the United States of America 179 12481024
2005 GRIP1 controls dendrite morphogenesis by regulating EphB receptor trafficking. Nature neuroscience 166 15965473
2006 Functional inhibitory cross-talk between constitutive androstane receptor and hepatic nuclear factor-4 in hepatic lipid/glucose metabolism is mediated by competition for binding to the DR1 motif and to the common coactivators, GRIP-1 and PGC-1alpha. The Journal of biological chemistry 158 16492670
2012 Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking. Neuron 157 22325201
2001 Factor recruitment and TIF2/GRIP1 corepressor activity at a collagenase-3 response element that mediates regulation by phorbol esters and hormones. The EMBO journal 140 11689447
1998 SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4. The Journal of biological chemistry 124 9812974
2005 The GRIP1:IRF3 interaction as a target for glucocorticoid receptor-mediated immunosuppression. The EMBO journal 123 16362036
2004 A direct functional link between the multi-PDZ domain protein GRIP1 and the Fraser syndrome protein Fras1. Nature genetics 120 14730302
2002 The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1. The Journal of biological chemistry 112 12060666
2005 Interactions between NEEP21, GRIP1 and GluR2 regulate sorting and recycling of the glutamate receptor subunit GluR2. The EMBO journal 93 16037816
2001 The glucocorticoid receptor interacting protein 1 (GRIP1) localizes in discrete nuclear foci that associate with ND10 bodies and are enriched in components of the 26S proteasome. Molecular endocrinology (Baltimore, Md.) 90 11266502
1998 Enhancement of estrogen receptor transcriptional activity by the coactivator GRIP-1 highlights the role of activation function 2 in determining estrogen receptor pharmacology. The Journal of biological chemistry 85 9506965
2012 Role of transcriptional coregulator GRIP1 in the anti-inflammatory actions of glucocorticoids. Proceedings of the National Academy of Sciences of the United States of America 80 22753499
2002 Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization. The Journal of biological chemistry 77 12493751
1999 An additional region of coactivator GRIP1 required for interaction with the hormone-binding domains of a subset of nuclear receptors. The Journal of biological chemistry 69 9920895
2010 GRIP1 and 2 regulate activity-dependent AMPA receptor recycling via exocyst complex interactions. Proceedings of the National Academy of Sciences of the United States of America 67 20956289
2005 GAC63, a GRIP1-dependent nuclear receptor coactivator. Molecular and cellular biology 65 15988012
2015 GRIP1 is required for homeostatic regulation of AMPAR trafficking. Proceedings of the National Academy of Sciences of the United States of America 63 26216979
2004 cAMP-dependent protein kinase regulates ubiquitin-proteasome-mediated degradation and subcellular localization of the nuclear receptor coactivator GRIP1. The Journal of biological chemistry 63 15347661
2003 Synergistic effects of coactivators GRIP1 and beta-catenin on gene activation: cross-talk between androgen receptor and Wnt signaling pathways. The Journal of biological chemistry 61 14638683
2020 GRIP1 regulates synaptic plasticity and learning and memory. Proceedings of the National Academy of Sciences of the United States of America 60 32948689
2012 Mutations in GRIP1 cause Fraser syndrome. Journal of medical genetics 60 22510445
2014 GRIP1 interlinks N-cadherin and AMPA receptors at vesicles to promote combined cargo transport into dendrites. Proceedings of the National Academy of Sciences of the United States of America 59 24639525
2002 Epidermolysis bullosa and embryonic lethality in mice lacking the multi-PDZ domain protein GRIP1. Proceedings of the National Academy of Sciences of the United States of America 57 11983858
1997 Yeast hormone response element assays detect and characterize GRIP1 coactivator-dependent activation of transcription by thyroid and retinoid nuclear receptors. Proceedings of the National Academy of Sciences of the United States of America 50 9108040
2000 GCN5 and ADA adaptor proteins regulate triiodothyronine/GRIP1 and SRC-1 coactivator-dependent gene activation by the human thyroid hormone receptor. Molecular endocrinology (Baltimore, Md.) 49 10809234
2005 Interaction of beta-catenin and TIF2/GRIP1 in transcriptional activation by the androgen receptor. The Journal of biological chemistry 48 16141201
2015 Activity-dependent synaptic GRIP1 accumulation drives synaptic scaling up in response to action potential blockade. Proceedings of the National Academy of Sciences of the United States of America 46 26109571
2004 A four PDZ domain-containing splice variant form of GRIP1 is localized in GABAergic and glutamatergic synapses in the brain. The Journal of biological chemistry 46 15226318
2019 The adaptor proteins HAP1a and GRIP1 collaborate to activate the kinesin-1 isoform KIF5C. Journal of cell science 39 31757889
2016 The transcriptional coregulator GRIP1 controls macrophage polarization and metabolic homeostasis. Nature communications 36 27464507
2005 GRIP1 in GABAergic synapses. The Journal of comparative neurology 36 15912503
2004 Association of GRIP1 with a GABA(A) receptor associated protein suggests a role for GRIP1 at inhibitory synapses. Biochemical pharmacology 36 15451408
2005 Differential use of functional domains by coiled-coil coactivator in its synergistic coactivator function with beta-catenin or GRIP1. The Journal of biological chemistry 35 16344550
2007 Supramodular nature of GRIP1 revealed by the structure of its PDZ12 tandem in complex with the carboxyl tail of Fras1. Journal of molecular biology 34 18155042
2002 Pure antiandrogens disrupt the recruitment of coactivator GRIP1 to colocalize with androgen receptor in nuclei. FEBS letters 34 12123801
2003 SNF2-related CBP activator protein (SRCAP) functions as a coactivator of steroid receptor-mediated transcription through synergistic interactions with CARM-1 and GRIP-1. Molecular endocrinology (Baltimore, Md.) 33 14500758
2010 Glucocorticoid receptor phosphorylation modulates transcription efficacy through GRIP-1 recruitment. Biochemistry 32 20047289
2017 Glucocorticoid-induced phosphorylation by CDK9 modulates the coactivator functions of transcriptional cofactor GRIP1 in macrophages. Nature communications 31 29170386
2014 The GRIP1/14-3-3 pathway coordinates cargo trafficking and dendrite development. Developmental cell 26 24576423
2011 Glucocorticoid-dependent phosphorylation of the transcriptional coregulator GRIP1. Molecular and cellular biology 25 22158970
2007 Orphan nuclear receptor TR2, a mediator of preadipocyte proliferation, is differentially regulated by RA through exchange of coactivator PCAF with corepressor RIP140 on a platform molecule GRIP1. Nucleic acids research 25 17389641
2005 GRIP1 mediates the interaction between the amino- and carboxyl-termini of the androgen receptor. Biological chemistry 24 15843149
2005 Role of activation function domain-1, DNA binding, and coactivator GRIP1 in the expression of partial agonist activity of glucocorticoid receptor-antagonist complexes. Biochemistry 23 15736964
2013 Acute BDNF treatment upregulates GluR1-SAP97 and GluR2-GRIP1 interactions: implications for sustained AMPA receptor expression. PloS one 22 23460828
2002 Regulation of GRIP1 and CBP Coactivator activity by Rho GDI modulates estrogen receptor transcriptional enhancement. The Journal of biological chemistry 22 12138084
2022 A Class I HDAC Inhibitor Rescues Synaptic Damage and Neuron Loss in APP-Transfected Cells and APP/PS1 Mice through the GRIP1/AMPA Pathway. Molecules (Basel, Switzerland) 21 35807406
2004 Nuclear hormone receptor coregulator GRIP1 suppresses, whereas SRC1A and p/CIP coactivate, by domain-specific binding of MyoD. The Journal of biological chemistry 20 15563453
2017 GRIP1 Binds to ApoER2 and EphrinB2 to Induce Activity-Dependent AMPA Receptor Insertion at the Synapse. Cell reports 19 28978486
2005 ErbB1 receptor ligands attenuate the expression of synaptic scaffolding proteins, GRIP1 and SAP97, in developing neocortex. Neuroscience 17 16226841
2000 Desethylamiodarone interferes with the binding of co-activator GRIP-1 to the beta 1-thyroid hormone receptor. FEBS letters 17 11007966
2019 Purkinje cell-specific Grip1/2 knockout mice show increased repetitive self-grooming and enhanced mGluR5 signaling in cerebellum. Neurobiology of disease 15 31476380
1998 Multiple receptor interaction domains of GRIP1 function in synergy. Nucleic acids research 15 9469826
2006 Identification and characterization of two novel splice forms of GRIP1 in the rat brain. Journal of neurochemistry 14 16539648
2006 Modulation of glucocorticoid receptor-interacting protein 1 (GRIP1) transactivation and co-activation activities through its C-terminal repression and self-association domains. The FEBS journal 14 16649994
2005 Generation of lentiviral transgenic rats expressing glutamate receptor interacting protein 1 (GRIP1) in brain, spinal cord and testis. Journal of neuroscience methods 14 16157387
2004 Analysis of two CBP (cAMP-response-element-binding protein-binding protein) interacting sites in GRIP1 (glucocorticoid-receptor-interacting protein), and their importance for the function of GRIP1. The Biochemical journal 14 15137909
2017 Mice lacking GRIP1/2 show increased social interactions and enhanced phosphorylation at GluA2-S880. Behavioural brain research 13 28063882
2016 The role of GRIP1 and ephrin B3 in blood pressure control and vascular smooth muscle cell contractility. Scientific reports 13 27941904
2015 Trip6 promotes dendritic morphogenesis through dephosphorylated GRIP1-dependent myosin VI and F-actin organization. The Journal of neuroscience : the official journal of the Society for Neuroscience 12 25673849
2021 EphrinB2 and GRIP1 stabilize mushroom spines during denervation-induced homeostatic plasticity. Cell reports 11 33789115
2016 LXRα represses LPS-induced inflammatory responses by competing with IRF3 for GRIP1 in Kupffer cells. International immunopharmacology 11 27085678
2001 Interaction of DNA polymerase beta with GRIP1 during meiosis. Chromosoma 10 11734998
2021 GLCCI1 Deficiency Induces Glucocorticoid Resistance via the Competitive Binding of IRF1:GRIP1 and IRF3:GRIP1 in Asthma. Frontiers in medicine 8 34504850
2013 cAMP response element-binding protein interacts with and stimulates the proteasomal degradation of the nuclear receptor coactivator GRIP1. Endocrinology 7 23462962
2021 Transcription cofactor GRIP1 differentially affects myeloid cell-driven neuroinflammation and response to IFN-β therapy. The Journal of experimental medicine 6 33045064
2002 Crystallization and preliminary X-ray crystallographic studies of the sixth PDZ domain of glutamate-receptor interacting protein 1 (GRIP1) from Rattus norvegicus. Acta crystallographica. Section D, Biological crystallography 1 12037318
2025 Dysregulated GluA2-Y876 phosphorylation contributes to loss of synaptic upscaling in GRIP1 mutant mice with reduced sociability and increased repetitive behavior. Molecular psychiatry 0 41390787
2024 LncRNA MSTRG.13,871/miR155-5p/Grip1 network involved in the post-cardiac arrest brain injury. Scientific reports 0 39443577
2024 [GRIP1 is Involved in the Interaction of Vimentin Filaments with Focal Adhesions in Endothelial Cells]. Molekuliarnaia biologiia 0 39970118
2009 [Liver X receptor alpha inhibits LPS-induced inflammation by down-regulating IFR3 and GRIP1 in mouse Kupffer cells]. Nan fang yi ke da xue xue bao = Journal of Southern Medical University 0 19460690
2007 No association of GRIP1 gene polymorphisms with schizophrenia in Chinese population. Progress in neuro-psychopharmacology & biological psychiatry 0 17303296