Abstract
The six‐transmembrane protein GDE2 induces the differentiation of postmitotic motor neurons by downregulating Notch in adjacent motor neuron progenitors. GDE2 function depends upon the integrity of its extracellular enzymatic domain that is homologous to bacterial glycerophosphodiester phosphodiesterases (GDPD). GDPDs metabolize glycerophosphodiesters into glycerol‐3‐phosphate and their corresponding alcohols, but it is unclear if and how GDE2 utilizes this mechanism to inhibit Notch activation. In this talk, I will discuss our recent observations that GDE2 regulates Notch signaling non cell autonomously, and that it does so through novel enzymatic mechanisms that control the surface availability of the Notch ligand Dll1.
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