ArticleFEBS letters2013
Tyrosine phosphorylation of the orphan receptor ESDN/DCBLD2 serves as a scaffold for the signaling adaptor CrkL.
Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Lactylation stabilizes DCBLD1 activating the pentose phosphate pathway to promote cervical cancer progression.Journal of experimental & clinical cancer research : CR · 2024Article
- Positive feedback between the T cell kinase Zap70 and its substrate LAT acts as a clustering-dependent signaling switch.Cell reports · 2021Article
- A homozygous nonsense mutation in DCBLD2 is a candidate cause of developmental delay, dysmorphic features and restrictive cardiomyopathy.Scientific reports · 2021Article
- FYN and ABL Regulate the Interaction Networks of the DCBLD Receptor Family.Molecular & cellular proteomics : MCP · 2020Article
- Association of DCBLD2 upregulation with tumor progression and poor survival in colorectal cancer.Cellular oncology (Dordrecht, Netherlands) · 2020Article
- An in silico proteomics screen to predict and prioritize protein-protein interactions dependent on post-translationally modified motifs.Bioinformatics (Oxford, England) · 2018Article
- Fyn-dependent phosphorylation of PlexinA1 and PlexinA2 at conserved tyrosines is essential for zebrafish eye development.The FEBS journal · 2018Article
- Dynamic multi-site phosphorylation by Fyn and Abl drives the interaction between CRKL and the novel scaffolding receptors DCBLD1 and DCBLD2.The Biochemical journal · 2017Article
- The neuropilin-like protein ESDN regulates insulin signaling and sensitivity.American journal of physiology. Heart and circulatory physiology · 2016Article
- Novel autophosphorylation sites of Src family kinases regulate kinase activity and SH2 domain-binding capacity.FEBS letters · 2016Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
A quantitative proteomics screen to identify substrates of the Src family of tyrosine kinases (SFKs) whose phosphorylation promotes CrkL-SH2 binding identified the known Crk-associated substrate (Cas) of Src as well as the orphan receptor endothelial and smooth muscle cell-derived neuropilin-like protein (ESDN). Mutagenesis analysis of ESDN's seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.
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