Marian B. Wilkin

TL;DR: The X-ray structure of a receptor binding region of a Notch ligand is reported and a highly conserved face of the DSL domain is revealed, suggesting that cis- and trans-regulation may occur through the formation of structurally distinct complexes that, unexpectedly, involve the same surfaces on both ligand and receptor.

TL;DR: This work shows in Drosophila that Notch signaling is limited by the activity of two Nedd4 family HECT domain proteins, Suppressor of deltex [Su(dx)] and DNedd4, and proposes a model in which endocytic sorting of Notch mediates a decision between its activation and downregulation.

TL;DR: HOPS/AP-3 contributions to Notch signaling during Drosophila midline formation and neurogenesis are uncovered and ways in which these endocytic pathways may modulate ligand-dependent and -independent events are discussed, as a mechanism that can potentiate NotCh signaling or dampen noise in the signaling network.

TL;DR: The dumpy gene encodes a gigantic extracellular molecule that is predicted to be a membrane-anchored fibre of almost a micrometer in length, which may provide a strong anchor for the underlying tissue, allowing it to maintain mechanical tension at sites under stress.

TL;DR: An intriguing pathway for the Notch signal has emerged where, after ligand-dependent proteolysis, an intracellular fragment of the receptor itself translocates to the nucleus to regulate gene expression.