The conserved transmembrane RING finger protein PLR-1 downregulates Wnt signaling by reducing Frizzled, Ror and Ryk cell-surface levels in C. elegans

• Published in: Development (Cambridge) Vol. 141; no. 3; pp. 617 - 628
• Main Authors: Moffat, Laura L, Robinson, Ryan E, Bakoulis, Anastasia, Clark, Scott G
• Format: Journal Article
• Language: English
• Published: England Company of Biologists 01.02.2014
• Subjects: Animals; Caenorhabditis elegans - cytology; Caenorhabditis elegans - metabolism; Caenorhabditis elegans Proteins - chemistry; Caenorhabditis elegans Proteins - metabolism; Cell Membrane - metabolism; Cell Movement; Cell Polarity; Conserved Sequence; Cytosol - metabolism; Down-Regulation; Endosomes - metabolism; Green Fluorescent Proteins - metabolism; Lysine - metabolism; Membrane Proteins - metabolism; Mutation - genetics; Neurons - cytology; Neurons - metabolism; Protein Structure, Secondary; Receptor Protein-Tyrosine Kinases - metabolism; Receptor Tyrosine Kinase-like Orphan Receptors - metabolism; RING Finger Domains; Structure-Activity Relationship; Ubiquitin-Protein Ligases - chemistry; Ubiquitin-Protein Ligases - metabolism; Wnt Signaling Pathway; Membrane protein trafficking; C. elegans; Wnt signaling; Neuronal polarity

Wnts control a wide range of essential developmental processes, including cell fate specification, axon guidance and anteroposterior neuronal polarization. We identified a conserved transmembrane RING finger protein, PLR-1, that governs the response to Wnts by lowering cell-surface levels of the Fri...