High impact information on lack

• Finally, we show that eIF4A acts synergistically with, but independently of, the ubiquitin ligase DSmurf, indicating that a dual system controls SMAD degradation [1].
• We conclude that dSmurf specifically targets phosphorylated MAD to proteasome-dependent degradation and regulates DPP signaling during development [2].
• Silencing of dSmurf using RNA interference stabilized MAD protein in Drosophila S2 cells [2].
• Smurf1: a link between cell polarity and ubiquitination [3].
• The DSmurf ubiquitin-protein ligase restricts BMP signaling spatially and temporally during Drosophila embryogenesis [4].

Biological context of lack

• After gastrulation, DSmurf mutations cause a temporal delay in downregulation of earlier DPP signals, resulting in a lethal defect in hindgut organogenesis [4].

Other interactions of lack

• dSmurf selectively degrades decapentaplegic-activated MAD, and its overexpression disrupts imaginal disc development [2].

References