Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion.

By R. Takada, Y. Satomi, Tomoko Kurata, N. Ueno, S. Norioka, H. Kondoh, Toshifumi Takao, S. Takada. Developmental Cell, 2006

794 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a61aad5e5702ea2622d90694e42c526db14d9f4c

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Citations in the corpus

Notum is required for neural and head induction via Wnt deacylation, oxidation and inactivation (2015, positive): “First, palmitoleoylation appears to be obligatory for Wnt secretion, as the Wnt3a(S209A) mutant, which has serine 209 substituted by an alanine, and thus lacks palmitoleoylation, is not secreted (Takada et al., 2006) possibly as a result of failure to bind to Wntless, a Wnt chaperone in the secretor”
Structural basis of WLS/Evi-mediated Wnt transport and secretion (2020, background): “A central feature of Wnt biology is the requirement for the covalent attachment of a monounsaturated palmitoleate (PAM) to a serine residue that is conserved in essentially all Wnts (Takada et al., 2006) (Figure 1A).”
Wnt/ b -Catenin Signaling, Disease, and Emerging Therapeutic Modalities (2017, background): “During synthesis, Wnt proteins, 40 kDa in size and rich in cysteines, are modified by attachment of a lipid, an acyl group termed palmitoleic acid (Willert et al., 2003; Rios-Esteves et al., 2014; Takada et al., 2006; Rios-Esteves andResh, 2013).”
Ghrelin octanoylation mediated by an orphan lipid transferase (2008, background): “(12) described that porcupine, an enzyme with structural similarities to membrane-bound O-acyl transferases (MBOAT), is required for serine-209 acylation with palmitoleic acid and for transport of Wnt3a from the endoplasmic reticulum for secretion.”
Identification of the acyltransferase that octanoylates ghrelin, an appetite-stimulating peptide hormone. (2008, positive): “Subsequent studies showed that Porcupine is required for the attachment of long-chain fatty acids to serine and cysteine residues in Wnt (Willert et al., 2003; Takada et al., 2006).”
Stereoselective fatty acylation is essential for the release of lipidated WNT proteins from the acyltransferase Porcupine (PORCN) (2019, background): “Although animals typically harbor multiple WNT genes, only a single WNT protein produced from an isolated cell line has been subjected to mass spectrometric analysis with the intention of identifying the adducted lipid (19).”
In vitro reconstitution of Wnt acylation reveals structural determinants of substrate recognition by the acyltransferase human Porcupine (2018, background): “Palmitoleic acid is a monounsaturated fatty acid, making Wnt the only known protein to be modified with such a lipid as well as the only known substrate of PORCN (7, 11).”
Inactivating mutations of RNF43 confer Wnt dependency in pancreatic ductal adenocarcinoma (2013, background): “Secretion of Wnt proteins requires Porcupine (PORCN), a membrane bound O-acyltransferase dedicated to Wnt posttranslational acylation (4, 5).”
Wnt/β-catenin signaling and disease. (2012, positive): “Loss of Porcupine leads to retention of Wnt3A in the ER (Takada et al., 2006) and a defect in Wg secretion in the Drosophila”
Wnt signaling and stem cell control (2008, background): “16-carbon fatty acid chain) attachment on a highly conserved serine residue (Willert et al. 2003; Takada et al. 2006; Komekado et al. 2007; Kurayoshi et al. 2007).”
Targeting Protein Lipidation in Disease (2012, background): “A multipass membrane protein termed Porcupine (Porcn) has been implicated in fatty acid modification of Wnt proteins [50, 52, 53].”