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Identification of the WNT1 residues required for palmitoylation by Porcupine
Author(s) -
Miranda M.,
Galli L.M.,
Enriquez M.,
Szabo L.A.,
Gao X.,
Hannoush R.N.,
Burrus L.W.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.11.016
Subject(s) - palmitoylation , wnt signaling pathway , microbiology and biotechnology , chemistry , biology , biochemistry , signal transduction , cysteine , enzyme
The post‐translational palmitoylation of WNT morphogens is critical for proper signaling during embryogenesis and adult homeostasis. The addition of palmitoyl groups to WNT proteins is catalyzed by Porcupine (PORCN). However, the Wnt amino acid residues required for recognition and palmitoylation by PORCN have not been fully characterized. We show that WNT1 residues 214–234 are sufficient for PORCN‐dependent palmitoylation of Ser224. Substitution of Ser224 with Thr, but not Cys, is tolerated in palmitoylation and biological assays. Our data highlight the importance of palmitoylation for WNT1 activity and establish PORCN as an O‐acyl transferase for WNT1.