The segment polarity gene porcupine encodes a putative multitransmembrane protein involved in Wingless processing.

By T. Kadowaki, E. Wilder, J. Klingensmith, K. Zachary, Norbert Perrimon. 1996

The Wnt protein Wingless (Wg) functions as a signal in patterning of both the Drosophila embryo and imaginal discs. Lack of porcupine (porc) activity is associated with mutant phenotypes similar to those of wg mutations. In porc mutant embryos, Wg protein is confined to the cells that produce it, suggesting that Porc plays a role in processing or secretion of Wg. porc encodes a novel transmembrane protein that appears to be concentrated at the endoplasmic reticulum. We present both genetic and in vitro evidence demonstrating that porc is involved specifically in the processing of Wg. We identified a human sequence related to Porc suggesting the existence of a family of proteins involved in processing of Wnts.

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Citations in the corpus

• Wnt/β-catenin signaling and disease. (2012, unknown): “Porc is a multipass transmembrane O-acyltransferase in the ER that is essential for Wnt palmitoylation and maturation (Hofmann, 2000; Kadowaki et al., 1996).”
• Precise Regulation of Porcupine Activity Is Required for Physiological Wnt Signaling (2012, background): “The first step in Wnt protein production is translation in the endoplasmic reticulum, followed by post-translational modification by the ERresident enzyme PORCN (16).”
• Wnt signaling in the intestinal epithelium: from endoderm to cancer. (2005, background): “This process may be mediated by Porcupine/MOM1; however, direct proof for this has not yet been provided (van den Heuvel et al. 1993; Kadowaki et al. 1996; Rocheleau et al. 1997).”
• The Wnt signaling pathway in development and disease. (2004, background): “The enzymes that add the palmitate to Wnts are likely to be encoded by the porcupine (por) gene in Drosophila (Kadowaki et al. 1996), called mom-1 in Caenorhabditis elegans (Rocheleau et al.”
• Prospective derivation of a Living Organoid Biobank of colorectal cancer patients (2015, background): “The O-acyltransferase Porcupine is required for the secretion of WNTs and its inhibition prevents autocrine/paracrine activation of the pathway (Kadowaki et al., 1996).”
• Wnts and Hedgehogs: lipid-modified proteins and similarities in signaling mechanisms at the cell surface (2003, background): “…be presented here, the reader is referred to various other reviews (Bienz and Clevers, 2000; Cadigan and Nusse, 1997; Ingham, 2001; Ingham and McMahon, 2001; Kalderon, 2000; Kalderon, 2002; McMahon, 2000; Moon et al., 2002) and the Wnt homepage (see http://www.stanford.edu/~rnusse/wntwindow.html).”
• Structural basis of WLS/Evi-mediated Wnt transport and secretion (2020, background): “Mutations in the Wnt palmitoleation site, inhibition of PORCN, or downregulation of WLS expression all prevent Wnt ER exit and secretion (Moti et al., 2019; Takada et al., 2006; Yu et al., 2014).”
• Osteoarthritis: pathogenic signaling pathways and therapeutic targets (2023, background): “The reduction of solubility of Wnt ligands strongly limits their physical signaling transduction capacity in different tissues and typically generates concentration gradients impacting adjacent cell behavior.(134,135) With both paracrine and autocrine effects, Wnt signaling was demonstrated to play ”
• Identification of the acyltransferase that octanoylates ghrelin, an appetite-stimulating peptide hormone. (2008, unknown): “Genetic studies in Drosophila had earlier demonstrated that Wingless activity required the action of another gene porcupine (Kadowaki et al., 1996).”
• Stearoyl CoA desaturase is required to produce active, lipid-modified Wnt proteins (2013, background): “Genetic (Kadowaki et al., 1996; Tanaka et al., 2000; van den Heuvel et al., 1993) and biochemical (Chen et al., 2009; Takada et al., 2006) studies have identified Porcupine (Porcn) as the acyltransferase responsible for lipid modification of Wnts. Porcn is a member of the membrane-bound…”