Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors.

@article{Dhalluin2000StructuralBO,
  title={Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors.},
  author={Christophe Dhalluin and Kelley S. Yan and O. S. Plotnikova and Keun Woo Lee and Lei Zeng and Miklos Kuti and Shiraz Mujtaba and Mitchell P Goldfarb and Ming Ming Zhou},
  journal={Molecular cell},
  year={2000},
  volume={6 4},
  pages={921-9}
}
SNT adaptor proteins transduce activation of fibroblast growth factor receptors (FGFRs) and neurotrophin receptors (TRKs) to common signaling targets. The SNT-1 phosphotyrosine binding (PTB) domain recognizes activated TRKs at a canonical NPXpY motif and, atypically, binds to nonphosphorylated FGFRs in a region lacking tyrosine or asparagine. Here, using NMR and mutational analyses, we show that the PTB domain utilizes distinct sets of amino acid residues to interact with FGFRs or TRKs in a… CONTINUE READING

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The SNT-1 phosphotyrosine binding ( PTB ) domain recognizes activated TRKs at a canonical NPXpY motif and , atypically , binds to nonphosphorylated FGFRs in a region lacking tyrosine or asparagine .
The SNT-1 phosphotyrosine binding ( PTB ) domain recognizes activated TRKs at a canonical NPXpY motif and , atypically , binds to nonphosphorylated FGFRs in a region lacking tyrosine or asparagine .
SNT adaptor proteins transduce activation of fibroblast growth factor receptors ( FGFRs ) and neurotrophin receptors ( TRKs ) to common signaling targets .
SNT adaptor proteins transduce activation of fibroblast growth factor receptors ( FGFRs ) and neurotrophin receptors ( TRKs ) to common signaling targets .
Our results suggest mechanisms by which SNTs serve as molecular switches to mediate the essential interplay between FGFR and TRK signaling during neuronal differentiation .
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