Affinage

GRIP1

Glutamate receptor-interacting protein 1 · UniProt Q9Y3R0

Length
1128 aa
Mass
122.4 kDa
Annotated
2026-06-10
78 papers in source corpus 40 papers cited in narrative 40 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

GRIP1 is a multi-domain scaffold protein that operates in two distinct cellular programs: nuclear receptor–dependent transcription and PDZ-mediated membrane-protein trafficking (PMID:8643509, PMID:24639525). As a p160-family transcriptional coactivator, GRIP1 binds the ligand-activated hormone-binding domains of steroid and class II nuclear receptors through three central LXXLL/NR-box motifs (with NR boxes II and III dominant and receptor-selective), bridging receptors to the basal machinery and to secondary coactivators such as p300 (PMID:8643509, PMID:9111344, PMID:9482670, PMID:9920895). The same GR-binding surface, combined with a distinct GRIP1 repression domain, redirects GRIP1 to act as a glucocorticoid receptor corepressor at AP-1 and NF-κB tethering response elements, defining a response-element-specific coactivator/corepressor switch (PMID:11689447, PMID:12481024); in vivo, this corepressor function restrains NF-κB-driven inflammatory cytokine genes in macrophages (PMID:22753499). This activator/corepressor balance is set by phosphorylation: glucocorticoid-induced, GR-dependent CDK9 phosphorylation of an N-terminal serine cluster potentiates coactivator output without affecting corepression (PMID:22158970, PMID:29170386). GRIP1 also serves nuclear receptor–independent transcription factors including HNF4, KLF4, IRF3, and β-catenin/Lef1 (PMID:9812974, PMID:27464507, PMID:16362036, PMID:14638683). In neurons, GRIP1 is a multi-PDZ adaptor enriched at the postsynaptic density that links GluA2-containing AMPA receptors, EphB receptors, and N-cadherin to the kinesin-1 motor KIF5 for dendritic transport, with motor engagement gated by phospho-dependent 14-3-3 binding at Thr956 (PMID:10436050, PMID:11986669, PMID:15965473, PMID:24576423, PMID:24639525); at synapses it controls activity-dependent and homeostatic AMPA-receptor recycling through the exocyst complex and through DHHC5/8-mediated palmitoylation of the GRIP1b isoform, governing LTP, synaptic scaling, and memory (PMID:20956289, PMID:22325201, PMID:26216979, PMID:32948689). Structurally, its PDZ modules act as supramodules and dimerization platforms underlying ligand recognition and multimerization (PMID:12493751, PMID:18155042). GRIP1 is genetically required for dermo-epidermal junction integrity via its interaction with the ECM protein Fras1, and biallelic GRIP1 mutations cause autosomal recessive Fraser syndrome in humans (PMID:11983858, PMID:14730302, PMID:18155042, PMID:22510445). A gain-of-function GRIP1 variant that strengthens GluA2 binding produces autism-like behaviors in mice, linking GRIP1-AMPAR coupling to neurodevelopmental disease (PMID:41390787).

Mechanistic history

Synthesis pass · year-by-year structured walk · 27 steps
  1. 1996 High

    Established GRIP1's founding identity by answering whether a dedicated factor bridges steroid receptors to transcription, defining it as a hormone-regulated coactivator.

    Evidence Yeast two-hybrid, in vitro binding, and reporter assays with GR/ER/AR hormone-binding domains

    PMID:8643509

    Open questions at the time
    • Did not map the receptor-binding motifs
    • Did not establish endogenous recruitment to native promoters
  2. 1998 High

    Resolved the molecular basis of receptor recognition by showing GRIP1 binds via central LXXLL NR-box motifs with receptor-specific box preferences, plus an auxiliary domain for a subset of receptors.

    Evidence Site-directed mutagenesis of LXXLL motifs with in vitro binding and reporter assays; cis-mapping of NIDaux

    PMID:9482670 PMID:9920895

    Open questions at the time
    • Did not determine in vivo occupancy at endogenous genes
    • Structural basis of box selectivity not solved
  3. 1999 High

    Revealed GRIP1's second cellular life by localizing it to the postsynaptic density and dendrites, implicating it in AMPA receptor targeting beyond transcription.

    Evidence Subcellular fractionation and immunogold electron microscopy of rat brain

    PMID:10436050

    Open questions at the time
    • No transport mechanism identified
    • Functional consequence of synaptic localization untested
  4. 2001 High

    Defined a context-dependent transcriptional switch by showing GRIP1 acts as a GR corepressor at tethering response elements using a distinct repression domain.

    Evidence Reporter assays, domain mapping, and dominant-negative analysis at collagenase-3 AP-1 GRE

    PMID:11689447 PMID:12481024

    Open questions at the time
    • Repression domain effector partners not identified
    • How element context selects activation vs repression unresolved at this stage
  5. 2002 High

    Identified the trafficking mechanism by showing GRIP1 directly couples AMPA-receptor cargo to kinesin heavy chains as a dendrite-steering motor adaptor.

    Evidence Yeast two-hybrid, co-IP, kinesin knockout and dominant-negative experiments in mice

    PMID:11986669

    Open questions at the time
    • Regulation of cargo loading/unloading not addressed
    • Other cargoes not yet defined
  6. 2002 High

    Established the structural logic of GRIP1's PDZ scaffold, showing PDZ6 uses a non-canonical residue for ligand contact and dimerizes to enable multimerization.

    Evidence X-ray crystallography of PDZ6 apo and liprin-α peptide complex

    PMID:12493751

    Open questions at the time
    • Higher-order assembly in vivo not visualized
    • Other PDZ domain specificities unresolved here
  7. 2002 High

    Demonstrated GRIP1's organismal essentiality and adhesion role through knockouts producing embryonic lethality with epidermolysis and reproductive defects.

    Evidence Knockout mice with histology and ultrastructural analysis of skin and reproductive organs

    PMID:11983858 PMID:12138202

    Open questions at the time
    • Molecular adhesion partners not identified in these studies
    • Tissue-specific contributions of transcriptional vs scaffold function not separated
  8. 2002 High

    Showed GRIP1 activity is tuned by post-translational modification, with SUMO-1 attachment in the NID modulating AR coactivation and nuclear colocalization.

    Evidence Sumoylation-site mutagenesis, confocal colocalization, and reporter assays

    PMID:12060666

    Open questions at the time
    • Dynamics and triggers of sumoylation not defined
    • Interplay with other modifications unaddressed
  9. 2004 High

    Identified the molecular cause of the skin/junction phenotype by showing GRIP1 binds and basally localizes the ECM protein Fras1, linking it to Fraser syndrome models.

    Evidence Pulldown/co-IP, Grip1 and eb-mouse genetics, and Fras1 immunolocalization

    PMID:14730302

    Open questions at the time
    • Structural binding interface not yet solved
    • Human relevance not established at this point
  10. 2005 High

    Broadened GRIP1's neuronal cargo repertoire and synaptic recycling roles by linking it to EphB transport, GABARAP, and NEEP21-dependent GluR2 recycling.

    Evidence RNAi rescue/dominant-negative, EphB triple-KO mice, in vitro binding, and electrophysiology

    PMID:15451408 PMID:15965473 PMID:16037816

    Open questions at the time
    • GABARAP interaction (Medium) lacks functional in vivo validation
    • How distinct cargoes are coordinated on one scaffold unresolved
  11. 2005 High

    Extended GRIP1's coregulator function beyond classical nuclear receptors by identifying IRF3 binding and competition that couples GRIP1 to innate immune transcription.

    Evidence Yeast two-hybrid, co-IP, GRIP1 knockdown/overexpression in macrophages, and MyD88/IFNAR-deficient mice

    PMID:14638683 PMID:15843149 PMID:16362036

    Open questions at the time
    • Mechanism of GR/IRF3 competition for GRIP1 not structurally defined
    • AR N/C bridging (Medium) from single lab
  12. 2007 High

    Provided the atomic basis for the Fras1 interaction by showing the PDZ12 supramodule presents PDZ1 for Fras1 binding, mechanistically tying GRIP1 to Fraser syndrome.

    Evidence X-ray crystallography of PDZ12-Fras1 peptide complex with domain-deletion binding assays

    PMID:18155042

    Open questions at the time
    • In vivo assembly with full-length Fras1 not visualized
  13. 2010 High

    Defined the synaptic recycling pathway by showing GRIP1-exocyst interaction is specifically required for activity-dependent, not basal, AMPA-receptor recycling.

    Evidence GRIP1/GRIP2 double conditional KO, electrophysiology, co-IP, and interaction-disruption epistasis

    PMID:20956289

    Open questions at the time
    • Exocyst subunit directly bound by GRIP1 not pinpointed
    • Coupling to upstream activity signals unresolved
  14. 2011 High

    Began resolving how the GRIP1 transcriptional switch is set by mapping glucocorticoid-induced, GR-dependent phosphorylation sites and their element-specific recruitment.

    Evidence Mass spectrometry phospho-mapping, phosphospecific antibodies, mutagenesis, ChIP, and kinase inhibitors

    PMID:22158970

    Open questions at the time
    • Definitive kinase identity left as candidates (CK2/CDK9)
    • Direct mechanism linking phosphorylation to activity not fully resolved here
  15. 2012 High

    Mechanistically resolved the inflammatory corepressor role by showing GRIP1 is required in macrophages for GR repression of NF-κB targets and protection from LPS shock.

    Evidence Conditional hematopoietic GRIP1 KO, genome-wide transcriptomics, and in vivo LPS challenge

    PMID:22753499

    Open questions at the time
    • Repression effector recruited by GRIP1 not identified
    • Distinction of corepressor vs coactivator surfaces at endogenous sites not fully resolved
  16. 2012 High

    Identified isoform-specific lipid regulation by showing DHHC5/8 palmitoylate GRIP1b to target it to endosomes and accelerate AMPA-receptor recycling.

    Evidence Palmitoylation/acyl-RAC assays, DHHC5/8 co-IP, endosomal imaging, and recycling assays

    PMID:22325201

    Open questions at the time
    • Link between palmitoylated GRIP1b and motor engagement only suggested
    • Depalmitoylating enzyme not defined
  17. 2012 Medium

    Confirmed human disease relevance by showing biallelic GRIP1 mutations segregate with Fraser syndrome in consanguineous families.

    Evidence Sequencing, RT-PCR of splice variant, and family segregation analysis

    PMID:22510445

    Open questions at the time
    • No in vitro functional rescue of patient alleles
    • Genotype-phenotype correlation limited to three families
  18. 2014 High

    Established regulated motor engagement by showing phospho-Thr956 14-3-3 binding detaches GRIP1 from kinesin-1 and a Thr956 mutation impairs dendritic development.

    Evidence Co-IP, Thr956 mutagenesis, and transgenic point-mutant mice with dendrite analysis

    PMID:24576423

    Open questions at the time
    • Upstream kinase controlling Thr956 not fully defined here
    • Spatial cue triggering detachment unknown
  19. 2014 High

    Demonstrated GRIP1 as a multilink cargo scaffold by showing simultaneous N-cadherin and GluA2 binding for cotransport on shared KIF5 vesicles to build synapses.

    Evidence Co-IP, live cotransport imaging, PDZ-disruption epistasis, and spine/synapse readouts

    PMID:24639525

    Open questions at the time
    • Stoichiometry of multi-cargo complexes unresolved
    • Selectivity of cargo loading not defined
  20. 2015 High

    Defined GRIP1's homeostatic plasticity role by showing it is required for synaptic scaling up via the GRIP1-GluA2 interaction.

    Evidence Genetic KO, shRNA knockdown-and-replace with GluA2-binding mutants, and mEPSC recordings

    PMID:26109571 PMID:26216979

    Open questions at the time
    • Mechanism driving GRIP1 synaptic accumulation (GluA2-independent) unresolved
    • Link to specific scaling signaling pathways unclear
  21. 2015 Medium

    Connected GRIP1 trafficking to actin-based motors by showing Trip6 and AKT1-phosphorylated Thr956 regulate GRIP1–myosin VI versus 14-3-3 partitioning in dendrite morphogenesis.

    Evidence Co-IP, RNAi, phospho-site mutagenesis, and dendritic morphology quantification

    PMID:25673849

    Open questions at the time
    • Single-lab co-IP evidence without in vivo genetic confirmation
    • Coordination between myosin VI and kinesin engagement unresolved
  22. 2016 High

    Revealed a GR-independent immunometabolic role by showing GRIP1 coactivates KLF4 for tissue-macrophage programming, with loss driving obesity-associated inflammation and insulin resistance.

    Evidence Conditional macrophage GRIP1 KO, GRIP1-KLF4 co-IP, ChIP, and metabolic phenotyping

    PMID:27464507

    Open questions at the time
    • Structural basis of KLF4-GRIP1 interaction undefined
    • Relationship to GRIP1 phospho-switch in this context untested
  23. 2017 High

    Resolved the transcriptional switch mechanism by identifying CDK9 in a GR:GRIP1:CDK9 complex that phosphorylates an N-terminal serine cluster to potentiate coactivation but not corepression.

    Evidence Kinase identification, phospho-site mutagenesis, ternary complex co-IP, ChIP, and CDK9 inhibition

    PMID:29170386

    Open questions at the time
    • How phospho-isoforms are excluded from transrepression sites mechanistically unclear
    • Phosphatase reversing the mark not identified
  24. 2017 High

    Expanded the postsynaptic scaffold by showing GRIP1 assembles an ApoER2-ephrinB2-AMPAR complex whose phospho-ephrinB2-dependent stability gates LTP.

    Evidence Complex co-IP, ephrinB2-Ser9 knock-in mice, LTP electrophysiology, and surface AMPAR assays

    PMID:28978486

    Open questions at the time
    • Direct GRIP1 binding site on ApoER2 not mapped
    • Hierarchy of complex assembly unresolved
  25. 2019 Medium

    Clarified how GRIP1 activates its motor by showing HAP1a-GRIP1 cooperatively relieve kinesin-1 autoinhibition at the hinge region.

    Evidence Co-IP from brain and in vitro kinesin activation reconstitution

    PMID:31757889

    Open questions at the time
    • Single-lab evidence without in vivo genetic validation
    • Structural detail of hinge stabilization unresolved
  26. 2020 High

    Established GRIP1's role in learning by showing GluA2 phospho-state (S880 down, Y876 up) tunes GRIP1-AMPAR association to drive LTP and memory.

    Evidence Grip1 conditional KO, LTP electrophysiology, phosphorylation assays, and behavioral testing

    PMID:32948689

    Open questions at the time
    • Kinases/phosphatases acting on GluA2-Y876/S880 not fully defined
    • Spatiotemporal coupling to receptor insertion unresolved
  27. 2025 High

    Linked GRIP1 to neurodevelopmental disease by showing a gain-of-function variant that strengthens GluA2 binding causes autism-like behavior and loss of synaptic upscaling.

    Evidence GRIP1-I507L knock-in mice with behavior, electrophysiology, and phospho-state immunoblots

    PMID:41390787

    Open questions at the time
    • Single knock-in allele; allelic series not tested
    • Human patient correlation not established here

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the transcriptional and trafficking functions of GRIP1 are partitioned within a cell, and what unifies its corepressor effector machinery, remain open.
  • Repression-domain effector partners unidentified
  • Isoform/compartment partitioning of nuclear vs neuronal functions undefined
  • Depalmitoylating and phosphatase enzymes for the regulatory switches unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0140110 transcription regulator activity 4 GO:0008092 cytoskeletal protein binding 3 GO:0005198 structural molecule activity 2
Localization
GO:0005634 nucleus 3 GO:0005768 endosome 2 GO:0005856 cytoskeleton 2 GO:0005886 plasma membrane 2 GO:0005654 nucleoplasm 1
Pathway
R-HSA-74160 Gene expression (Transcription) 4 R-HSA-168256 Immune System 3 R-HSA-9609507 Protein localization 3 R-HSA-112316 Neuronal System 2 R-HSA-162582 Signal Transduction 2 R-HSA-5653656 Vesicle-mediated transport 2
Complex memberships
ApoER2-ephrinB2-AMPAR postsynaptic complexGR:GRIP1:CDK9 transcription complexexocyst complex (interaction)kinesin-1 (KIF5) motor-adaptor complex

Evidence

Reading pass · 40 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1996 GRIP1 (glucocorticoid receptor-interacting protein 1) physically interacts with the hormone binding domains (HBDs) of glucocorticoid, estrogen, and androgen receptors in a hormone-regulated manner, and contains a transcriptional activation domain capable of activating reporter genes; it functions as a transcriptional coactivator bridging steroid receptor HBDs and the RNA polymerase II basal transcription machinery. Yeast two-hybrid, in vitro binding assay, reporter gene assay in yeast and mammalian cells, squelching/dominant-negative overexpression Proceedings of the National Academy of Sciences of the United States of America High 8643509
1997 Full-length GRIP1 interacts in a hormone-dependent manner with HBDs of all five steroid receptors and class II nuclear receptors (TRα, VDR, RARα, RXRα); antagonists do not promote GR-GRIP1 interaction. GRIP1 coactivates the AF-2 but not AF-1 transactivation domain of GR, demonstrating that AF-1 and AF-2 use distinct coactivator mechanisms. Yeast two-hybrid, in vitro binding, reporter gene assay in yeast and mammalian cells, GR truncation and point mutants Molecular and cellular biology High 9111344
1998 GRIP1 binds nuclear receptors via three LXXLL motifs (NR Boxes) in its central region; NR Box II and NR Box III are crucial for most NR binding activity, with different NRs showing distinct NR Box preferences (ER more dependent on Box II; AR and GR more dependent on Box III). Mutagenesis of LXXLL motifs, in vitro binding assay, yeast two-hybrid, reporter gene assay Molecular endocrinology (Baltimore, Md.) High 9482670
1998 GRIP1 associates with hepatocyte nuclear factor 4 (HNF4) in vivo and enhances its transactivation; the AF-2 domain of HNF4 is required for this interaction. GRIP1 also cooperates with p300 to augment HNF4 activity and enhances expression from the HNF1 promoter in an HNF4-binding-site-dependent manner. Co-immunoprecipitation, reporter gene assay, transient transfection The Journal of biological chemistry Medium 9812974
1999 GRIP1 contains an auxiliary NR interaction domain (NIDaux, aa 1011–1121) beyond the central NID that is required in cis for efficient interaction with a subset of NRs (GR, AR, RARα) but not others (PR, RXRα, TRβ1, VDR). The NIDaux region contains the p300 interaction domain, but this function is separable from the NR-binding contribution. In vitro binding assay, yeast two-hybrid, mammalian co-transfection with deletion/point mutants The Journal of biological chemistry High 9920895
1999 GRIP1 and GRIP2 are enriched in synaptic plasma membrane and postsynaptic density fractions of rat brain and localize in a somatodendritic pattern in neurons; GRIP1 is enriched in dendritic spines near the postsynaptic density, in dendritic shafts, and in peri-Golgi regions, consistent with a role in AMPA receptor targeting. Subcellular fractionation, immunohistochemistry, electron microscopy (DAB and immunogold) The Journal of neuroscience High 10436050
2001 At the collagenase-3 AP-1 tethering GRE, GRIP1 is recruited and functions as a GR corepressor (not coactivator); this requires the same GR-binding surface of GRIP1 used for coactivation but also a distinct GRIP1 repression domain. A GRIP1 fragment containing the GR-interacting region acts as a dominant-negative for repression. Reporter gene assay, GRIP1 domain mapping/mutants, dominant-negative overexpression The EMBO journal High 11689447
2001 GRIP1 localizes in discrete intranuclear foci dependent on its C-terminal activation domains (AD1 and AD2); a subpopulation of foci associate with ND10/PML bodies via the AD1 (CBP-interacting) domain; GRIP1 foci are enriched in 26S proteasome components and GRIP1 is degraded by the proteasome, as shown by proteasome inhibitor lactacystin. GFP-fusion live-cell imaging, confocal microscopy, proteasome inhibitor treatment, fluorescence intensity measurement Molecular endocrinology (Baltimore, Md.) Medium 11266502
2002 GRIP1 directly interacts with kinesin heavy chains and steers kinesin to dendrites as a motor adaptor for AMPA receptors; gene targeting and dominant-negative experiments in mice show that disruption of kinesin heavy chains causes abnormal GRIP1 localization, and overexpression of the kinesin-binding domain of GRIP1 causes accumulation of endogenous kinesin in the somatodendritic area. Yeast two-hybrid, co-immunoprecipitation, gene targeting (knockout mouse), dominant-negative overexpression, immunofluorescence localization Nature High 11986669
2002 At the AP-1 tethering GRE (collagenase-3) and NF-κB tethering GRE (IL-8 gene), GR and GRIP1 use a distinct GRIP1 corepression domain not present in SRC1 or RAC3; at the osteocalcin GRE (direct DNA binding repression), both GRIP1 and SRC1 corepressed and the GRIP1-specific domain was dispensable. GR thus engages distinct GRIP1 surfaces in a response-element-specific manner. Reporter gene assay with GRIP1 deletion/point mutants, domain mapping, comparison with p160 family members Proceedings of the National Academy of Sciences of the United States of America High 12481024
2002 SUMO-1 is covalently attached to GRIP1 at lysines 239, 731, and 788; Lys-731 and Lys-788 are in the NR interaction domain and their mutation impairs colocalization of GRIP1 with androgen receptor in nuclei and attenuates GRIP1 coactivation of AR-dependent transcription. GRIP1 sumoylation is mediated by PIAS proteins. Mutagenesis of sumoylation sites, confocal colocalization, reporter gene assay, co-immunoprecipitation The Journal of biological chemistry High 12060666
2002 Crystal structure of GRIP1 PDZ6 domain alone and in complex with the C-terminal peptide of liprin-α was determined at 1.5 and 1.8 Å; PDZ6 uses Ile-736 (not the conserved Leu) for hydrophobic contact with the ligand's -2 Tyr, forms an antiparallel dimer through a site distal to the peptide-binding groove, enabling GRIP multimerization. X-ray crystallography (1.5 Å and 1.8 Å resolution structures) The Journal of biological chemistry High 12493751
2002 Genetic deletion of GRIP1 in mice results in embryonic lethality around E12 with extensive skin blistering (epidermolysis bullosa phenotype) due to cleavage below the lamina densa at the dermo-epidermal junction, demonstrating that GRIP1 PDZ scaffold is essential for dermo-epidermal junction integrity. Knockout mouse generation, histology, electron microscopy of blisters Proceedings of the National Academy of Sciences of the United States of America High 11983858
2002 GRIP1 deletion in mice lacking mTIF2/GRIP1 causes male hypofertility due to spermiogenesis defects (teratozoospermia) and age-dependent testicular degeneration, with TIF2 expression essential for Sertoli cell adhesion to germ cells; female hypofertility results from placental hypoplasia requiring maternal TIF2 in decidua stromal cells. Knockout mouse (TIF2−/− mice), histology, phenotypic analysis of reproductive organs Molecular and cellular biology High 12138202
2004 GRIP1 physically interacts with the extracellular matrix protein Fras1 and is required for Fras1 localization to the basal side of cells; loss of GRIP1 causes Fraser syndrome-like defects (subepidermal blisters, renal agenesis, syndactyly, cryptophthalmos) in mice, and the eye-blebs mouse Fraser syndrome model has a deletion of two GRIP1 coding exons. Co-immunoprecipitation/pulldown (GRIP1-Fras1 interaction), genetic mouse models (Grip1 KO and eb mouse), immunofluorescence localization of Fras1 Nature genetics High 14730302
2004 PKA activation induces ubiquitination and proteasomal degradation of GRIP1, reducing its half-life; PKA also stimulates recruitment of GRIP1 to subnuclear foci colocalizing with proteasomes. Ubiquitin-activating E1 enzyme is required for PKA-mediated GRIP1 degradation (established using ts20 thermolabile E1 cells). Pulse-chase experiment, proteasome inhibitors (MG132, lactacystin), co-immunoprecipitation with ubiquitin, ts20 temperature-sensitive E1 cell line, GFP-GRIP1 live imaging The Journal of biological chemistry High 15347661
2005 GRIP1 knockdown by siRNA in hippocampal neurons causes loss of dendrites with mislocalization of GluR2, EphB2, and KIF5; loss-of-dendrite phenotype is rescued by overexpression of extracellular EphB2 domain, phenocopied by dominant-negative EphB2 intracellular domain, and impaired EphB2 trafficking by disrupting KIF5-GRIP1 interaction strongly impairs dendritic growth. GRIP1 thus acts as an adaptor for kinesin-dependent EphB receptor transport to dendrites. RNAi knockdown, rescue/dominant-negative overexpression, immunofluorescence, EphB triple-KO mice Nature neuroscience High 15965473
2005 GRIP1 interacts with GABARAP (a GABA-A receptor γ2 subunit-associated protein) directly through PDZ domains 4–6 of GRIP1, as shown by in vitro pull-down and co-immunoprecipitation; GRIP1 colocalizes with γ2-containing GABA-A receptors in cultured hippocampal neurons, suggesting a role at inhibitory synapses. In vitro protein interaction assay, co-immunoprecipitation, immunofluorescence colocalization Biochemical pharmacology Medium 15451408
2005 GRIP1 mediates the N/C terminal interaction of androgen receptor by bridging AR amino-terminal domain (NTD) and ligand-binding domain (LBD) simultaneously; GRIP1 mutants lacking either AR interaction domain cannot restore AR N/C interaction, indicating that GRIP1 bridges the two AR termini to stabilize the complex and facilitate secondary cofactor recruitment. Co-immunoprecipitation, reporter gene assay with AR and GRIP1 mutants Biological chemistry Medium 15843149
2005 NEEP21 (a neuronal endosomal protein) associates with GRIP1 and the AMPA receptor subunit GluR2; NEEP21-GRIP1 interaction is regulated by neuronal activity. Disrupting this interaction (by NEEP21 fragment expression) decreases surface GluR2, delays recycling of internalized GluR2 to early endosomes and lysosomes, and reduces GluR2-containing AMPAR at synapses. Co-immunoprecipitation, atomic force microscopy, surface receptor assay, electrophysiology (inward rectification of AMPAR-mediated responses) The EMBO journal High 16037816
2005 GRIP1 interacts with IRF3 (interferon regulatory factor 3) through its corepression domain; endogenous GRIP1 and IRF3 interact in mammalian cells; GR and IRF3 compete for GRIP1 binding, and GR activation or GRIP1 knockdown blocks IRF3-dependent gene expression, while GRIP1 overexpression rescues it. GRIP1 thus serves as a cofactor in innate immunity via the TLR3-IRF3 pathway. Yeast two-hybrid (GRIP1 corepression domain screen), co-immunoprecipitation, GRIP1 knockdown/overexpression in macrophages, MyD88/IFNAR-deficient mice The EMBO journal High 16362036
2003 GRIP1 and β-catenin bind strongly to each other through the AD2 domain of GRIP1 and synergistically enhance AR and Lef1 transcriptional activity; GRIP1 can only bind AR directly but is recruited to Lef1 indirectly through β-catenin. Both coactivators are recruited to AR-driven and Lef1-driven promoters. Co-immunoprecipitation, reporter gene assay, chromatin immunoprecipitation (ChIP) The Journal of biological chemistry High 14638683
2007 Crystal structure of GRIP1 PDZ12 tandem in complex with the Fras1 C-terminal peptide shows that PDZ1 folding strictly depends on covalent attachment to PDZ2 (supramodule); only the PDZ1 peptide-binding groove contacts Fras1. This structural basis explains GRIP1-Fras1 interaction and links to Fraser syndrome. X-ray crystallography of PDZ12 tandem + Fras1 peptide complex, domain deletion binding assays Journal of molecular biology High 18155042
2010 GRIP1 and GRIP2 interact with the exocyst protein complex; loss of both GRIP1 and GRIP2 in neurons does not affect basal AMPA-R steady-state trafficking or endocytosis, but specifically impairs activity-dependent AMPA-R recycling. Disruption of GRIP1-exocyst binding causes the same recycling deficit. Conditional knockout (GRIP1 KO in postnatal neurons from GRIP2 KO mice), electrophysiology, co-immunoprecipitation (GRIP1-exocyst), dominant-negative disruption of GRIP1-exocyst interaction 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; two putative kinases are casein kinase 2 and CDK9. Phosphorylation is functionally relevant to GR-activated transcription and to response element-specific recruitment of phospho-GRIP1 to native GR targets, as shown with phosphospecific antibodies and mutagenesis. Mass spectrometry phosphorylation mapping, phosphospecific antibodies, site-directed mutagenesis, chromatin immunoprecipitation, kinase inhibitor experiments Molecular and cellular biology High 22158970
2012 DHHC5 and DHHC8 palmitoyl acyltransferases specifically palmitoylate GRIP1b; palmitoylation requires a PDZ ligand unique to DHHC5/8. Palmitoylated GRIP1b is targeted to trafficking endosomes and may link endosomes to kinesin motors; palmitoylation increases GRIP1b's ability to accelerate AMPA-R recycling. GRIP1b palmitoylation turnover rate is among the highest reported. Palmitoylation assay, co-immunoprecipitation (DHHC5/8-GRIP1b), immunofluorescence (endosomal targeting), AMPA-R recycling assay, acyl-RAC palmitoylation capture Neuron High 22325201
2012 GRIP1 depletion specifically in hematopoietic macrophages (conditional KO) attenuates GR-mediated repression of NF-κB target cytokine genes in a dose-dependent manner; GRIP1-deficient mice are sensitized to LPS-induced shock; genome-wide analysis shows broad derepression of LPS-induced GC-sensitive targets without affecting LPS-induced activation. GRIP1 is required for GR corepressor function at NF-κB sites. Conditional hematopoietic GRIP1 KO mouse, genome-wide transcriptome analysis, LPS challenge in vivo, macrophage gene expression Proceedings of the National Academy of Sciences of the United States of America High 22753499
2012 Human GRIP1 mutations (splice site mutation causing exon 17 skipping with frameshift, and a 4-bp deletion) segregate with Fraser syndrome in an autosomal recessive manner in three unrelated consanguineous families, genetically confirming GRIP1 as a Fraser syndrome gene in humans. Genetic sequencing, RT-PCR of mRNA splice variant, family segregation analysis Journal of medical genetics Medium 22510445
2014 GRIP1 binds 14-3-3 proteins in a phospho-dependent manner at Thr956; 14-3-3 binding detaches GRIP1 from the kinesin-1 motor complex, regulating cargo transport. A Thr956 point mutation in transgenic mice impairs dendritic development. GRIP1 is thus a regulated kinesin adaptor whose motor engagement is controlled by phosphorylation. Co-immunoprecipitation, Thr956 mutagenesis, transgenic mouse (T956 point mutant), dendritic morphology analysis Developmental cell High 24576423
2014 GRIP1 simultaneously binds N-cadherin (via PDZ domain 2) and GluA2-containing AMPARs (via other PDZ domains); both cargoes are presorted to identical transport vesicles for dendrite delivery and are cotransported by KIF5 using GRIP1 as a multilink scaffold. Interference with either cargo's PDZ binding or KIF5 motor impairs turnover of both cargoes and reduces spine number and excitatory synapses. Co-immunoprecipitation, live imaging cotransport, dominant-negative PDZ binding disruption, microtubule depolymerization, AMPAR exocytosis blockade Proceedings of the National Academy of Sciences of the United States of America High 24639525
2015 GRIP1 expression is bidirectionally altered by neuronal activity; GRIP1 redistributes to synaptic sites and its binding to GluA2 changes during synaptic scaling. Loss of GRIP1 blocks accumulation of surface AMPARs and scaling up in response to chronic activity blockade; the interaction between GRIP1 and GluA2 is specifically required for scaling up. Biochemical fractionation, genetic GRIP1 KO, electrophysiology (AMPAR mEPSCs), knockdown-and-replace with GluA2-binding mutant 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 amplitudes; shRNA GRIP1 knockdown prevents scaling up; scaling up requires the GRIP1-GluA2 interaction, but GRIP1's synaptic accumulation during scaling up does not require GluA2 binding. shRNA knockdown, overexpression, knockdown-and-replace with GRIP1 and GluA2 mutants, electrophysiology (mEPSC recording) Proceedings of the National Academy of Sciences of the United States of America High 26109571
2016 GRIP1 serves as a coactivator for KLF4, a driver of tissue-resident macrophage differentiation, via a GR-independent pathway; conditional GRIP1 KO in macrophages impairs IL4-induced macrophage programming, causes massive macrophage infiltration and inflammation in adipose tissue, fatty liver, hyperglycemia, and insulin resistance in obese mice. Conditional macrophage GRIP1 KO mouse, co-immunoprecipitation (GRIP1-KLF4), ChIP, gene expression analysis, metabolic phenotyping Nature communications High 27464507
2017 CDK9 phosphorylates GRIP1 at an N-terminal serine cluster; GC treatment recruits CDK9 into GR:GRIP1:CDK9 hetero-complexes, producing GRE-specific GRIP1 phospho-isoforms. Phosphorylation potentiates GRIP1 coactivator but not corepressor properties; phospho-GRIP1 and CDK9 are absent at GR transrepression sites near pro-inflammatory genes. Kinase identification, phospho-site mutagenesis, co-immunoprecipitation of GR:GRIP1:CDK9 complex, ChIP, CDK9 inhibition, phosphospecific antibodies Nature communications High 29170386
2017 GRIP1 binds ApoER2 and bridges a postsynaptic complex including ApoER2, ephrinB2, and AMPA receptors; phosphorylation of ephrinB2 Ser-9 is essential for complex stability; in vivo mutation of ephrinB2 Ser-9 disrupts the complex and impairs activity-induced AMPA receptor insertion and LTP. Co-immunoprecipitation (GRIP1-ApoER2-ephrinB2-AMPAR complex), knock-in mouse (ephrinB2-Ser9 mutation), LTP electrophysiology, surface AMPAR insertion assay Cell reports High 28978486
2019 HAP1a and GRIP1 form a protein complex in the brain and co-operate to activate the kinesin-1 subunit KIF5C in vitro, with HAP1a and GRIP1 together stabilizing the central hinge region of kinesin-1 that is critical for its autoinhibition. Co-immunoprecipitation from brain, in vitro kinesin activation assay Journal of cell science Medium 31757889
2020 GRIP1 is recruited into synapses during LTP; deletion of Grip1 in neurons blocks synaptic AMPAR accumulation induced by glycine-mediated depolarization and impairs hippocampal LTP, as well as learning and memory in mice. Phosphorylation of GluA2-S880 is decreased and phosphorylation of GluA2-Y876 is elevated during chem-LTP, enhancing GRIP1-AMPAR association and AMPAR insertion into the postsynaptic membrane. Grip1 conditional KO mouse, electrophysiology (LTP), immunofluorescence, biochemical phosphorylation assays, learning/memory behavioral tests Proceedings of the National Academy of Sciences of the United States of America High 32948689
2015 Trip6 interacts with GRIP1 and myosin VI; phosphorylation of GRIP1-Thr956 by AKT1 inhibits the GRIP1-myosin VI interaction and facilitates GRIP1 binding to 14-3-3, regulating F-actin organization and dendritic morphogenesis. Depletion of Trip6, GRIP1, or myosin VI each impairs dendritic morphology. Co-immunoprecipitation, RNAi knockdown, phospho-site mutagenesis, F-actin staining, dendritic morphology quantification The Journal of neuroscience Medium 25673849
2025 A gain-of-function GRIP1 variant (I586L/murine I507L) that increases GluA2 binding is sufficient to cause impaired social interaction, increased repetitive behaviors, and increased neuronal excitability in mice; basal phosphorylation of GluA2-Y876 is elevated, blocking further induction by inactivity and causing loss of synaptic upscaling, while GluA2-S880 phosphorylation (regulating Hebbian plasticity) is unaffected. Knock-in mouse (GRIP1-I507L), behavioral testing, electrophysiology, immunoblot of phosphorylation state Molecular psychiatry High 41390787
2013 CREB directly interacts with GRIP1 (via CREB's bZIP domain) and stimulates proteasomal degradation of ubiquitinated GRIP1; CREB is required for PKA-stimulated GRIP1 degradation; CREB-mediated GRIP1 downregulation affects expression of a subset of ER-α-regulated genes. CREB Ser-133 phosphorylation or transcriptional activity is not required for GRIP1 interaction. Co-immunoprecipitation, ubiquitination assay, domain-mapping mutagenesis, GRIP1 protein level measurement in MCF-7 cells Endocrinology Medium 23462962

Source papers

Stage 0 corpus · 78 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
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 600 8643509
1997 GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Molecular and cellular biology 483 9111344
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
2002 The function of TIF2/GRIP1 in mouse reproduction is distinct from those of SRC-1 and p/CIP. Molecular and cellular biology 212 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 180 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 161 16492670
2012 Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking. Neuron 158 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 125 9812974
2005 The GRIP1:IRF3 interaction as a target for glucocorticoid receptor-mediated immunosuppression. The EMBO journal 124 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 84 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 70 9920895
2005 GAC63, a GRIP1-dependent nuclear receptor coactivator. Molecular and cellular biology 69 15988012
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 68 20956289
2020 GRIP1 regulates synaptic plasticity and learning and memory. Proceedings of the National Academy of Sciences of the United States of America 63 32948689
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
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 39 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
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.) 34 14500758
2002 Pure antiandrogens disrupt the recruitment of coactivator GRIP1 to colocalize with androgen receptor in nuclei. FEBS letters 34 12123801
2017 Glucocorticoid-induced phosphorylation by CDK9 modulates the coactivator functions of transcriptional cofactor GRIP1 in macrophages. Nature communications 33 29170386
2010 Glucocorticoid receptor phosphorylation modulates transcription efficacy through GRIP-1 recruitment. Biochemistry 32 20047289
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
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) 23 35807406
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
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 16 31476380
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 15 16649994
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
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

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