ArticleFEBS letters2016
Novel autophosphorylation sites of Src family kinases regulate kinase activity and SH2 domain-binding capacity.
Article in FEBS letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- CoDIAC: A comprehensive approach for interaction analysis provides insights into SH2 domain function and regulation.Science signaling · 2025Article
- CoDIAC: A comprehensive approach for interaction analysis reveals novel insights into SH2 domain function and regulation.bioRxiv : the preprint server for biology · 2025Article
- Reversible ubiquitination conferred by domain shuffling controls paired NLR immune receptor complex homeostasis in plant immunity.Nature communications · 2025Article
- ExploringMicrobial cell (Graz, Austria) · 2021Review
- Quantitative phosphoproteomics uncovers dysregulated kinase networks in Alzheimer's disease.Nature aging · 2021Article
- Direct cysteine sulfenylation drives activation of the Src kinase.Nature communications · 2018Article
- Article
- In Vivo Phosphoproteome Analysis Reveals Kinome Reprogramming in Hepatocellular Carcinoma.Molecular & cellular proteomics : MCP · 2018Article
- Fyn-dependent phosphorylation of PlexinA1 and PlexinA2 at conserved tyrosines is essential for zebrafish eye development.The FEBS journal · 2018Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
Src family tyrosine kinases (SFKs) are critical players in normal and aberrant biological processes. While phosphorylation importantly regulates SFKs at two known tyrosines, large-scale phosphoproteomics have revealed four additional tyrosines commonly phosphorylated in SFKs. We found these novel tyrosines to be autophosphorylation sites. Mimicking phosphorylation at the C-terminal site to the activation loop decreased Fyn activity. Phosphomimetics and direct phosphorylation at the three SH2 domain sites increased Fyn activity while reducing phosphotyrosine-dependent interactions. While 68% of human SH2 domains exhibit conservation of at least one of these tyrosines, few have been found phosphorylated except when found in cis to a kinase domain.
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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.