Structural and functional consequences of tyrosine phosphorylation in the LRP1 cytoplasmic domain.

@article{Betts2008StructuralAF,
  title={Structural and functional consequences of tyrosine phosphorylation in the LRP1 cytoplasmic domain.},
  author={Gina N Betts and Peter van der Geer and Elizabeth A. Komives},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 23},
  pages={15656-64}
}
The cytoplasmic domain of LRP1 contains two NPXY motifs that have been shown to interact with signaling proteins. In previous work, we showed that Tyr(4507) in the distal NPXY motif is phosphorylated by v-Src, whereas denaturation of the protein was required for phosphorylation of Tyr(4473) in the membraneproximal NPXY motif. Amide H/D exchange studies… CONTINUE READING