High impact information on edl

• Depolymerization of Yan by Mae represents a novel mechanism of transcriptional control that sensitizes Yan for regulation by receptor tyrosine kinases [1].
• Phosphorylation and downregulation of Yan is facilitated by a protein called Mae [1].
• Mae mediates MAP kinase phosphorylation of Ets transcription factors in Drosophila [2].
• Mae is essential for the normal development and viability of Drosophila, and is required in vivo for normal signalling of the epidermal growth factor receptor [2].
• Antagonistic regulation of Yan nuclear export by Mae and Crm1 may increase the stringency of the Ras response [3].

Biological context of edl

• However, EDL/MAE functions as an antagonist of Pointed P2, by binding to its Pointed domain and abolishing its transcriptional activation function [4].
• Here we report the cloning and characterization of a new component of this signal transduction pathway called Mae (for modulator of the activity of Ets) [2].
• After activation, transcriptional up-regulation of Mae apparently leads to complete depolymerization and export of Yan [3].

Anatomical context of edl

• The loss of EDL/MAE function results in reduced number of photoreceptor neurons and chordotonal organs, suggesting a positive role in the induction by Spitz EGF [4].

Physical interactions of edl

• Mae binding to Pnt-P2 occludes this docking surface, thereby acting to downregulate Pnt-P2 activity [5].

Regulatory relationships of edl

• We propose that EDL/MAE blocks autocrine activation of Pointed P2 so that inducing cells remain induction-competent [4].

Other interactions of edl

• We describe developmental roles of a novel negative regulator of Ras signaling, EDL/MAE, a protein with an Ets-specific Pointed domain but not an ETS DNA-binding domain [4].
• Derepression by depolymerization; structural insights into the regulation of Yan by Mae [1].

References