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Newly revealed ShcD has been characterized as an intracellular phosphotyrosine adaptor protein belonging to the Src homology and collagen (Shc) family. These scaffolding molecules facilitate receptor-mediated signal transduction through their ability to selectively recognize and bind, via PTB and SH2 domains, to phosphorylated tyrosine residues in the cytoplasmic tails of a variety of activated receptors. A central CH1 domain couples to downstream signaling molecules including Grb2. ShcD is most similar in form to ShcA; however, unlike the latter, its expression in the mouse is localized to the brain and skeletal muscle. Consistent with this observation, we report that human ShcD is able to bind the TrkA neurotrophin receptor responsive to nerve growth factor (NGF). This interaction is similar to that of other Shc proteins in that it is strongly influenced by the TrkA Tyr 490 residue, and results in ShcD phosphorylation. Surprisingly, we find that both the PTB and SH2 domains of ShcD impact its ability to complex with TrkA, in contrast to the PTB-mediated interaction documented for traditional Shc proteins. TrkA binding analyses performed with different ShcD mutants suggest that the contributions of the PTB and SH2 domains supercede simple co operativity, and are in fact reminiscent of auto-regulatory mechanisms. Here we report both the canonical and atypical characteristics of the ShcD / TrkA interaction, including novel proposed models of adaptor-receptor interactions.

The ShcD phosphotyrosine adaptor protein exhibits novel binding characteristics with the TrkA neurotrophin receptor