Data from: Proteolytic processing of palmitoylated Hedgehog peptides specifies the 3-4 intervein region of the Drosophila wing

Cell fate determination during development often requires morphogen
transport from producing to distant responding cells. Hedgehog (Hh)
morphogens present a challenge to this concept, as all Hhs are synthesized
as terminally lipidated molecules that form insoluble clusters at the
surface of producing cells. While several proposed Hh transport modes tie
directly into these unusual properties, the crucial step of Hh relay from
producing cells to receptors on remote responding cells remains
unresolved. Using wing development in Drosophila melanogaster as a model,
we show that Hh relay and direct patterning of the 3-4 intervein region
strictly depend on proteolytic removal of lipidated N-terminal membrane
anchors. Site-directed modification of the N-terminal Hh processing site
selectively eliminated the entire 3-4 intervein region, and additional
targeted removal of N-palmitate restored its formation. Hence,
palmitoylated membrane anchors restrict morphogen spread until
site-specific processing switches membrane-bound Hh into bioactive forms
with specific patterning functions.