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Fig. 4. Wnt and Hedgehog (Hh) acylation and the role of Porc and Rasp. (A) The
palmitoylation of wild-type Wnt and Hh proteins. Wnt is palmitoylated through
a thioesther to a cysteine. Dashed lines indicate the possibility of
disulphide formation between other cysteines in Wnts. Hh is palmitoylated
through an amide on the N-terminal cysteine. The two other cysteines in Hh are
not disulphide linked and have free sulfhydryl (SH) groups. (B) In the absence
of Porc, Wnt is not palmitoylated on the first cysteine. This cysteine then
has a free SH group that interferes with disulphide formation between other
cysteines. The resulting protein is midfolded and will not be secreted. In the
absence of Rasp, the first cysteine in Hh is not palmitoylated but the number
of free SH groups does not change and the Hh protein is still secreted.
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