Protein-serine O-palmitoleoyltransferase porcupine

Definition:

Protein-serine O-palmitoleoyltransferase that acts as a key regulator of the Wnt signaling pathway by mediating the attachment of palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1(9Z)), to Wnt proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors.

References:

[1]. Xinxin Gao, et al. Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine. Nat Chem Biol. 2014 Jan;10(1):61-8. [Content Brief]

[2]. Gary S Coombs, et al. WLS-dependent secretion of WNT3A requires Ser209 acylation and vacuolar acidification. J Cell Sci. 2010 Oct 1;123(Pt 19):3357-67. [Content Brief]

[3]. Andrea Caricasole, et al. Molecular cloning and initial characterization of the MG61/PORC gene, the human homologue of the Drosophila segment polarity gene Porcupine. Gene. 2002 Apr 17;288(1-2):147-57. [Content Brief]

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