[HTML][HTML] Structural and functional consequences of tyrosine phosphorylation in the LRP1 cytoplasmic domain
GN Betts, P van der Geer, EA Komives - Journal of biological chemistry, 2008 - ASBMB
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 reveal that the distal NPXY motif is fully solvent-exposed, whereas the proximal one
is not. Phosphopeptide mapping combined with in vitro and in vivo kinase experiments show …
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 reveal that the distal NPXY motif is fully solvent-exposed, whereas the proximal one
is not. Phosphopeptide mapping combined with in vitro and in vivo kinase experiments show …