The direct association of the multiple PDZ domain containing proteins (MUPP‐1) with the human c‐Kit C‐terminus is regulated by tyrosine kinase activity

@article{Mancini2000TheDA,
  title={The direct association of the multiple PDZ domain containing proteins (MUPP‐1) with the human c‐Kit C‐terminus is regulated by tyrosine kinase activity},
  author={A. Mancini and A. Koch and M. Stefan and H. Niemann and T. Tamura},
  journal={FEBS Letters},
  year={2000},
  volume={482}
}
  • A. Mancini, A. Koch, +2 authors T. Tamura
  • Published 2000
  • Chemistry, Medicine
  • FEBS Letters
    • We have identified the multiple PDZ domain containing protein (MUPP‐1 or MPDZ) as a novel binding partner of the human c‐Kit. c‐Kit binds specifically to the 10th PDZ domain of MUPP‐1 via its C‐terminal sequence. Furthermore, a kinase negative‐mutant receptor interacted more strongly with MUPP‐1 than the wild‐type c‐Kit. Strikingly, a constitutively activated c‐Kit (D816V‐Kit) did not bind to MUPP‐1, although this oncogenic form retains the PDZ binding motif ‘HDDV’ at the C‐terminal end… CONTINUE READING
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    References

    SHOWING 1-10 OF 28 REFERENCES
    Cloning and characterization of MUPP1, a novel PDZ domain protein
    • 180
    Activating mutation in the catalytic domain of c-kit elicits hematopoietic transformation by receptor self-association not at the ligand-induced dimerization site.
    • 73
    Human proto‐oncogene c‐kit: a new cell surface receptor tyrosine kinase for an unidentified ligand.
    • 1,472
    PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor.
    • 204
    • PDF
    The C‐terminus of the kinase‐defective neuregulin receptor ErbB‐3 confers mitogenic superiority and dictates endocytic routing
    • 105
    • PDF
    Tyrosine Phosphorylation of the Juxtamembrane Domain of the v-Fms Oncogene Product Is Required for Its Association with a 55-kDa Protein*
    • 31
    • PDF
    Identification, sequence, and mapping of the mouse multiple PDZ domain protein gene, Mpdz.
    • 16
    Direct interaction of nerve growth factor receptor, TrkA, with non‐receptor tyrosine kinase, c‐Abl, through the activation loop
    • 27
    • PDF
    Interaction between Gab1 and the c-Met receptor tyrosine kinase is responsible for epithelial morphogenesis
    • 557
    Identification of a second Grb2 binding site in the v-Fms tyrosine kinase
    • 50
    • PDF