ArticleOpen biology2021
Determination of the membrane topology of PORCN, an O-acyl transferase that modifies Wnt signalling proteins.
Article in Open biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- The Roles of ProteinCancer communications (London, England) · 2026Review
- Mechanistic insights into Wnt-β-catenin pathway activation and signal transduction.Nature reviews. Molecular cell biology · 2025Review
- Molecular pathways and targeted therapies in head and neck cancers pathogenesis.Frontiers in oncology · 2024Review
- Cellular Uptake of a Fluorescent Ligand Reveals GhrelinACS chemical biology · 2023Article
- The role of Evi/Wntless in exporting Wnt proteins.Development (Cambridge, England) · 2023Review
- Case Report: Papillary thyroid carcinoma in Goltz-Gorlin syndrome.Frontiers in endocrinology · 2023Article
- A rising tide lifts all MBOATs: recent progress in structural and functional understanding of membrane boundFrontiers in physiology · 2023Review
- Gone with the Wnt(less): a mechanistic perspective on the journey of Wnt.Biochemical Society transactions · 2022Article
- Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Wnt gradients elicit distinct cellular responses, such as proliferation, specification, differentiation and survival in a dose-dependent manner. Porcupine (PORCN), a membrane-bound O-acyl transferase (MBOAT) that resides in the endoplasmic reticulum, catalyses the addition of monounsaturated palmitate to Wnt proteins and is required for Wnt gradient formation and signalling. In humans, PORCN mutations are causal for focal dermal hypoplasia (FDH), an X-linked dominant syndrome characterized by defects in mesodermal and endodermal tissues. PORCN is also an emerging target for cancer therapeutics. Despite the importance of this enzyme, its structure remains poorly understood. Recently, the crystal structure of DltB, an MBOAT family member from bacteria, was solved. In this report, we use experimental data along with homology modelling to DltB to determine the membrane topology of PORCN. Our studies reveal that PORCN has 11 membrane domains, comprising nine transmembrane spanning domains and two reentrant domains. The N-terminus is oriented towards the lumen while the C-terminus is oriented towards the cytosol. Like DltB, PORCN has a funnel-like structure that is encapsulated by multiple membrane-spanning helices. This new model for PORCN topology allows us to map residues that are important for biological activity (and implicated in FDH) onto its three-dimensional structure.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.