High impact information on rasp

• Our results suggest that Rasp-dependent acylation is necessary to generate a fully active Hh protein [1].
• Loss-of-function mutations in cmn cause similar patterning defects to those caused by hh or dispatched (disp) mutations [2].
• Moreover, cmn affects the expression of hh responsive genes but not of hh itself [2].
• Like disp, cmn acts upstream of patched (ptc) and its activity is required only in the Hh secreting cells [2].
• However, unlike disp, which is required for the release of the cholesterol-modified form of Hh, cmn regulates the activity of Hh in a manner that is independent of cholesterol modification [2].

Anatomical context of rasp

• In cultured cells, Rasp promotes palmitate addition to the N-terminal cysteine residue of Spitz, and this cysteine is required for Spitz activity in vivo [3].

Other interactions of rasp

• In addition, we identified a novel component in the hh pathway, which we name central missing (cmn) [2].

References