ArticleMolecular and cellular biology2013
Homodimerization of the Wnt receptor DERAILED recruits the Src family kinase SRC64B.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Src acts with WNT/FGFRL signaling to pattern the planarian anteroposterior axis.Development (Cambridge, England) · 2022Article
- ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes.Cell reports · 2021Article
- RYK-mediated filopodial pathfinding facilitates midgut elongation.Development (Cambridge, England) · 2020Article
- Midline axon guidance in the Drosophila embryonic central nervous system.Seminars in cell & developmental biology · 2019Review
- Screening for transmembrane association in divisome proteins using TOXGREEN, a high-throughput variant of the TOXCAT assay.Biochimica et biophysica acta · 2016Article
- The Formin DAAM Functions as Molecular Effector of the Planar Cell Polarity Pathway during Axonal Development in Drosophila.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Ror2 as a therapeutic target in cancer.Pharmacology & therapeutics · 2015Review
- On the electrostatic properties of homodimeric proteins.Journal of theoretical & computational chemistry · 2014Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ryk pseudokinase receptors act as important transducers of Wnt signals, particularly in the nervous system. Little is known, however, of their interactions at the cell surface. Here, we show that a Drosophila Ryk family member, DERAILED (DRL), forms cell surface homodimers and can also heterodimerize with the two other fly Ryks, DERAILED-2 and DOUGHNUT ON 2. DERAILED homodimerization levels increase significantly in the presence of its ligand, WNT5. In addition, DERAILED displays ligand-independent dimerization mediated by a motif in its transmembrane domain. Increased dimerization of DRL upon WNT5 binding or upon the replacement of DERAILED's extracellular domain with the immunoglobulin Fc domain results in an increased recruitment of the Src family kinase SRC64B, a previously identified downstream pathway effector. Formation of the SRC64B/DERAILED complex requires SRC64B's SH2 domain and DERAILED's PDZ-binding motif. Mutations in DERAILED's inactive tyrosine kinase-homologous domain also disrupt the formation of DERAILED/SRC64B complexes, indicating that its conformation is likely important in facilitating its interaction with SRC64B. Finally, we show that DERAILED's function during embryonic axon guidance requires its Wnt-binding domain, a putative juxtamembrane extracellular tetrabasic cleavage site, and the PDZ-binding domain, indicating that DERAILED's activation involves a complex set of events including both dimerization and proteolytic processing.
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