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Gene Review

GRIP1  -  glutamate receptor interacting protein 1

Homo sapiens

Synonyms: GRIP-1, Glutamate receptor-interacting protein 1
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Disease relevance of GRIP1

  • PATIENTS: 92 children, born since 1976, who had meningomyelocele and hydrocephalus and were treated at the University of Rochester Medical Center. METHODS: Grip and pinch strength were measured between July, 1991, and June, 2003 [1].

High impact information on GRIP1

  • These results indicate that NEEP21-GRIP1 binding is crucial for GluR2-AMPAR sorting through endosomes and their recruitment to the plasma membrane, providing a first molecular mechanism to differentially regulate AMPAR subunit cycling in internal compartments [2].
  • This methylation mark of p300 GBD is removed by peptidyl deiminase 4, thereby enhancing the p300-GRIP1 interaction [3].
  • In vitro, the F domain was found to obscure an AF-2-independent binding site for GRIP1 that did not map to nuclear receptor boxes II or III [4].
  • The loss of ligand-dependent transactivation for some mutants can largely be reversed in the presence of GRIP1, which acts as a strong ligand-dependent coactivator for wild-type T3R alpha [5].
  • Here we show that an about 85-kDa protein kinase phosphorylates GRIP1 on serine 917 [6].

Biological context of GRIP1

  • Inhibition of endogenous TIF1alpha expression reduced transcriptional activation by the GRIP1 N-terminal domain but not by the CARM1 C-terminal domain, suggesting that TIF1alpha may be more important for mediating the activity of the former than the latter [7].
  • This study investigated whether GRIP1 genetic polymorphisms (rs1038923 and rs4913301) cause a predisposal to schizophrenia [8].
  • Results demonstrated that neither single marker nor haplotype analysis revealed an association between variants at the GRIP1 locus and schizophrenia, suggesting that it is unlikely that the GRIP1 polymorphisms investigated play a substantial role in conferring susceptibility to schizophrenia [8].
  • We show here that ERRalpha1 represses ERalpha-mediated activation in MCF-7 cells because it failed to recruit the coactivator glucocorticoid receptor interacting protein 1 (GRIP1) when bound to an estrogen response element [9].
  • Phosphorylation of glutamate receptor interacting protein 1 regulates surface expression of glutamate receptors [6].

Anatomical context of GRIP1

  • Likewise, coexpression of GluR2 together with full-length wild type GRIP1 enhances GluR2 surface expression in fibroblasts, whereas full-length GRIP1-S917D had no effect [6].

Associations of GRIP1 with chemical compounds

  • VP16-ERalpha and c-Jun, which both interact with GRIP1, had synergistic effect on GAL4-GRIP1-induced transcription in the presence of estradiol, and this synergistic effect was not observed with the ERalpha mutant VP16-ER241G or when c-Fos, which bound GRIP1 but not ERalpha, was used instead of c-Jun [10].
  • Therefore, GRIP1, previously found to interact with the glucocorticoid, estrogen, and androgen receptors, may also have a role in T3R alpha-mediated ligand-dependent transcriptional activation [5].
  • It is now generally considered that calpain activation is necessary for LTP formation in the cleavage of substrates such as protein kinase Czeta, NMDA receptors, and the glutamate receptor-interacting protein [11].
  • METHODS: Coated split crimpable hooks (Never-Slip Grip, TP Orthodontics, LaPorte, Ind), ribbed crimpable hooks (TP Orthodontics), and .032-in brass soldered hooks/notched electrodes (Ormco/Sybron Dental Specialties, Orange, Calif) were attached to a 0.019 x 0.025-in stainless steel archwire [12].
  • Development of Hand Function and Precision Grip Control in Individuals With Cerebral Palsy: A 13-Year Follow-up Study [13].

Physical interactions of GRIP1

  • These studies demonstrate that SHP does not inhibit CAR-mediated trans-activation by interfering with DNA binding or by competition with GRIP1 [14].
  • Furthermore, using coimmunoprecipitation assays we show that GABARAP interacts with GRIP1 in vivo [15].
  • To better understand the structural basis of peptide recognition by a class II PDZ domain and PDZ-mediated multimerization, we determined the crystal structures of the GRIP1 PDZ6 domain alone and in complex with a synthetic C-terminal octapeptide of human liprin-alpha at resolutions of 1.5 and 1.8 A, respectively [16].
  • Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein [17].

Regulatory relationships of GRIP1

  • Instead, SHP may either inhibit recruitment of other coactivators by GRIP1 or actively recruit corepressors directly to the CAR/RXR/PBRU complex [14].

Other interactions of GRIP1


Analytical, diagnostic and therapeutic context of GRIP1

  • Co-immunoprecipitation experiments demonstrate that PPAR alpha and GRIP1/TIF2 physically interact in vivo in human liver [20].
  • Here we show that GRIP1 contains at least two receptor-interacting regions using the hormone-binding domain of several receptors as bait in the yeast two-hybrid assay [21].
  • GRIP1e 4-7 is a 75 kDa 4-PDZ-domain variant of GRIP1, containing the 12 amino acid C-terminus originally described for the 7-PDZ-domain GRIP1a/b. Northern blots indicated that GRIP1d mRNA is 5.1 kb long and abundant in brain [22].
  • METHODS: Grip strength (n = 986) and appendicular muscle mass (n = 328, using dual-energy x-ray absorptiometry) were obtained in 1995 and 1996 and repeated after a 3-year follow-up [23].


  1. Do grip and pinch strength predict neurologic complications in children with spina bifida and hydrocephalus? Liptak, G.S., Fried, R., Baltus-Hebert, E., Eyer Tierney, S., Fucile, S., Doremus, T.L. Pediatric neurosurgery. (2006) [Pubmed]
  2. Interactions between NEEP21, GRIP1 and GluR2 regulate sorting and recycling of the glutamate receptor subunit GluR2. Steiner, P., Alberi, S., Kulangara, K., Yersin, A., Sarria, J.C., Regulier, E., Kasas, S., Dietler, G., Muller, D., Catsicas, S., Hirling, H. EMBO J. (2005) [Pubmed]
  3. Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination. Lee, Y.H., Coonrod, S.A., Kraus, W.L., Jelinek, M.A., Stallcup, M.R. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  4. Modulation of transcriptional activation and coactivator interaction by a splicing variation in the F domain of nuclear receptor hepatocyte nuclear factor 4alpha1. Sladek, F.M., Ruse, M.D., Nepomuceno, L., Huang, S.M., Stallcup, M.R. Mol. Cell. Biol. (1999) [Pubmed]
  5. Mutations in the conserved C-terminal sequence in thyroid hormone receptor dissociate hormone-dependent activation from interference with AP-1 activity. Saatcioglu, F., Lopez, G., West, B.L., Zandi, E., Feng, W., Lu, H., Esmaili, A., Apriletti, J.W., Kushner, P.J., Baxter, J.D., Karin, M. Mol. Cell. Biol. (1997) [Pubmed]
  6. Phosphorylation of glutamate receptor interacting protein 1 regulates surface expression of glutamate receptors. Kulangara, K., Kropf, M., Glauser, L., Magnin, S., Alberi, S., Yersin, A., Hirling, H. J. Biol. Chem. (2007) [Pubmed]
  7. Transcriptional intermediary factor 1alpha mediates physical interaction and functional synergy between the coactivator-associated arginine methyltransferase 1 and glucocorticoid receptor-interacting protein 1 nuclear receptor coactivators. Teyssier, C., Ou, C.Y., Khetchoumian, K., Losson, R., Stallcup, M.R. Mol. Endocrinol. (2006) [Pubmed]
  8. No association of GRIP1 gene polymorphisms with schizophrenia in Chinese population. Tsai, S.J., Liou, Y.J., Liao, D.L., Cheng, C.Y., Hong, C.J. Prog. Neuropsychopharmacol. Biol. Psychiatry (2007) [Pubmed]
  9. Estrogen-Related Receptor {alpha}1 Transcriptional Activities Are Regulated in Part via the ErbB2/HER2 Signaling Pathway. Ariazi, E.A., Kraus, R.J., Farrell, M.L., Jordan, V.C., Mertz, J.E. Mol. Cancer Res. (2007) [Pubmed]
  10. Characterization of the physical interaction between estrogen receptor alpha and JUN proteins. Teyssier, C., Belguise, K., Galtier, F., Chalbos, D. J. Biol. Chem. (2001) [Pubmed]
  11. Proteases involved in long-term potentiation. Tomimatsu, Y., Idemoto, S., Moriguchi, S., Watanabe, S., Nakanishi, H. Life Sci. (2002) [Pubmed]
  12. Comparison of torsional stability of 2 types of split crimpable surgical hooks with soldered brass surgical hooks. O'Bannon, S.P., Dunn, W.J., Lenk, J.S. American journal of orthodontics and dentofacial orthopedics : official publication of the American Association of Orthodontists, its constituent societies, and the American Board of Orthodontics. (2006) [Pubmed]
  13. Development of Hand Function and Precision Grip Control in Individuals With Cerebral Palsy: A 13-Year Follow-up Study. Eliasson, A.C., Forssberg, H., Hung, Y.C., Gordon, A.M. Pediatrics (2006) [Pubmed]
  14. Repression of CAR-mediated transactivation of CYP2B genes by the orphan nuclear receptor, short heterodimer partner (SHP). Bae, Y., Kemper, J.K., Kemper, B. DNA Cell Biol. (2004) [Pubmed]
  15. Association of GRIP1 with a GABA(A) receptor associated protein suggests a role for GRIP1 at inhibitory synapses. Kittler, J.T., Arancibia-Carcamo, I.L., Moss, S.J. Biochem. Pharmacol. (2004) [Pubmed]
  16. Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization. Im, Y.J., Park, S.H., Rho, S.H., Lee, J.H., Kang, G.B., Sheng, M., Kim, E., Eom, S.H. J. Biol. Chem. (2003) [Pubmed]
  17. Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein. Matsuda, S., Mikawa, S., Hirai, H. J. Neurochem. (1999) [Pubmed]
  18. Crystal structure of the human LRH-1 DBD-DNA complex reveals Ftz-F1 domain positioning is required for receptor activity. Solomon, I.H., Hager, J.M., Safi, R., McDonnell, D.P., Redinbo, M.R., Ortlund, E.A. J. Mol. Biol. (2005) [Pubmed]
  19. Suturing techniques of surgeons utilizing two different needle-holder grips. Seki, S. Am. J. Surg. (1988) [Pubmed]
  20. Negative regulation of human fibrinogen gene expression by peroxisome proliferator-activated receptor alpha agonists via inhibition of CCAAT box/enhancer-binding protein beta. Gervois, P., Vu-Dac, N., Kleemann, R., Kockx, M., Dubois, G., Laine, B., Kosykh, V., Fruchart, J.C., Kooistra, T., Staels, B. J. Biol. Chem. (2001) [Pubmed]
  21. Multiple receptor interaction domains of GRIP1 function in synergy. Schmidt, S., Baniahmad, A., Eggert, M., Schneider, S., Renkawitz, n.u.l.l. Nucleic Acids Res. (1998) [Pubmed]
  22. Identification and characterization of two novel splice forms of GRIP1 in the rat brain. Charych, E.I., Li, R., Serwanski, D.R., Li, X., Miralles, C.P., Pinal, N., De Blas, A.L. J. Neurochem. (2006) [Pubmed]
  23. Inflammatory markers and loss of muscle mass (sarcopenia) and strength. Schaap, L.A., Pluijm, S.M., Deeg, D.J., Visser, M. Am. J. Med. (2006) [Pubmed]
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