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Gene Review

MAGI3  -  membrane associated guanylate kinase, WW...

Homo sapiens

Synonyms: KIAA1634, MAGI-3, Membrane-associated guanylate kinase inverted 3, Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3, dJ730K3.2
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Disease relevance of MAGI3

  • In glioblastoma SF763T cells MAGI-3 was associated with a tyrosine-phosphorylated protein with the apparent molecular weight of 130 kDa, whereas in Caco2 cells it was associated with a 90 kDa protein [1].
  • In the present work, we demonstrate the specific interaction between LPA(2) and MAGI-3, and the effects of MAGI-3 in colon cancer cells using SW480 as a cell model [2].

High impact information on MAGI3

  • Moreover, two novel beta1AR-interacting proteins, SAP97 and MAGI-3, were also identified [3].
  • Full-length beta1AR robustly associated with full-length MAGI-3 in cells, and this association was abolished by mutation of the beta1AR terminal valine residue to alanine (V477A), as determined by co-immunoprecipitation experiments and immunofluorescence co-localization studies [3].
  • MAGI-3 co-expression with beta1AR profoundly impaired beta1AR-mediated ERK1/2 activation but had no apparent effect on beta1AR-mediated cyclic AMP generation or agonist-promoted beta1AR internalization [3].
  • These data suggest that MAGI3 allows for the juxtaposition of PTEN/MMAC to phospholipid signaling pathways involved with cell survival [4].
  • In this study, we show that a multi-PDZ containing protein, MAGI-3, specifically binds to frizzled-4 and -7 [5].

Anatomical context of MAGI3


Associations of MAGI3 with chemical compounds

  • Although MAGI-3 itself was not phosphorylated on tyrosine residues, it became associated with tyrosine-phosphorylated proteins following a short treatment of the cells with vanadate [1].

Physical interactions of MAGI3

  • Junctional protein MAGI-3 interacts with receptor tyrosine phosphatase beta (RPTP beta) and tyrosine-phosphorylated proteins [1].

Regulatory relationships of MAGI3

  • These results demonstrate that MAGI-3 interacts directly with LPA(2) and regulates the ability of LPA(2) to activate Erk and RhoA [2].

Other interactions of MAGI3

  • Oncogenic human papillomavirus E6 proteins target the MAGI-2 and MAGI-3 proteins for degradation [9].
  • The interaction between RPTP beta and MAGI-3 was confirmed by co-immunoprecipitation and pulldown experiments in transfected cells [1].
  • The 10a scaffold inhibited the interaction between MAGI-3 and PTEN and showed cellular activities that are consistent with the inhibition of NHERF-1 function [10].

Analytical, diagnostic and therapeutic context of MAGI3


  1. Junctional protein MAGI-3 interacts with receptor tyrosine phosphatase beta (RPTP beta) and tyrosine-phosphorylated proteins. Adamsky, K., Arnold, K., Sabanay, H., Peles, E. J. Cell. Sci. (2003) [Pubmed]
  2. MAGI-3 regulates LPA-induced activation of Erk and RhoA. Zhang, H., Wang, D., Sun, H., Hall, R.A., Yun, C.C. Cell. Signal. (2007) [Pubmed]
  3. Proteomic analysis of beta1-adrenergic receptor interactions with PDZ scaffold proteins. He, J., Bellini, M., Inuzuka, H., Xu, J., Xiong, Y., Yang, X., Castleberry, A.M., Hall, R.A. J. Biol. Chem. (2006) [Pubmed]
  4. Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase. Wu, Y., Dowbenko, D., Spencer, S., Laura, R., Lee, J., Gu, Q., Lasky, L.A. J. Biol. Chem. (2000) [Pubmed]
  5. MAGI-3 is involved in the regulation of the JNK signaling pathway as a scaffold protein for frizzled and Ltap. Yao, R., Natsume, Y., Noda, T. Oncogene (2004) [Pubmed]
  6. MAGI-1: a widely expressed, alternatively spliced tight junction protein. Laura, R.P., Ross, S., Koeppen, H., Lasky, L.A. Exp. Cell Res. (2002) [Pubmed]
  7. Identification of MAGI-3 as a transforming growth factor-alpha tail binding protein. Franklin, J.L., Yoshiura, K., Dempsey, P.J., Bogatcheva, G., Jeyakumar, L., Meise, K.S., Pearsall, R.S., Threadgill, D., Coffey, R.J. Exp. Cell Res. (2005) [Pubmed]
  8. Human T-cell leukemia virus type 1 Tax oncoprotein induces and interacts with a multi-PDZ domain protein, MAGI-3. Ohashi, M., Sakurai, M., Higuchi, M., Mori, N., Fukushi, M., Oie, M., Coffey, R.J., Yoshiura, K., Tanaka, Y., Uchiyama, M., Hatanaka, M., Fujii, M. Virology (2004) [Pubmed]
  9. Oncogenic human papillomavirus E6 proteins target the MAGI-2 and MAGI-3 proteins for degradation. Thomas, M., Laura, R., Hepner, K., Guccione, E., Sawyers, C., Lasky, L., Banks, L. Oncogene (2002) [Pubmed]
  10. Rational design of a nonpeptide general chemical scaffold for reversible inhibition of PDZ domain interactions. Fujii, N., Haresco, J.J., Novak, K.A., Gage, R.M., Pedemonte, N., Stokoe, D., Kuntz, I.D., Kiplin Guy, R. Bioorg. Med. Chem. Lett. (2007) [Pubmed]
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