ArticleProceedings of the National Academy of Sciences of the United States of America2012
Modified SH2 domain to phototrap and identify phosphotyrosine proteins from subcellular sites within cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- New insights on the regulators and inhibitors of RhoA-ROCK signalling in Parkinson's disease.Metabolic brain disease · 2025Review
- RhoA-ROCK2 signaling possesses complex pathophysiological functions in cancer progression and shows promising therapeutic potential.Cancer cell international · 2024Review
- RhoA Signaling in Neurodegenerative Diseases.Cells · 2022Review
- The functional landscape of the human phosphoproteome.Nature biotechnology · 2020Article
- Essential role for InSyn1 in dystroglycan complex integrity and cognitive behaviors in mice.eLife · 2019Article
- RHO Family GTPases in the Biology of Lymphoma.Cells · 2019Review
- Tyrosyl phosphorylation of KRAS stalls GTPase cycle via alteration of switch I and II conformation.Nature communications · 2019Article
- Photoaffinity-engineered protein scaffold for systematically exploring native phosphotyrosine signaling complexes in tumor samples.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Regulation of RhoA GTPase and various transcription factors in the RhoA pathway.Journal of cellular physiology · 2018Review
- Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors.Small GTPases · 2018Review
- Identification of an elaborate complex mediating postsynaptic inhibition.Science (New York, N.Y.) · 2016Article
- Tyrosine glycosylation of Rho by Yersinia toxin impairs blastomere cell behaviour in zebrafish embryos.Nature communications · 2015Article
- Article
- Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A phosphotyrosine switch for cargo sequestration at clathrin-coated buds.The Journal of biological chemistry · 2014Article
- The genesis of tyrosine phosphorylation.Cold Spring Harbor perspectives in biology · 2014Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Spatial regulation of tyrosine phosphorylation is important for many aspects of cell biology. However, phosphotyrosine accounts for less than 1% of all phosphorylated substrates, and it is typically a very transient event in vivo. These factors complicate the identification of key tyrosine kinase substrates, especially in the context of their extraordinary spatial organization. Here, we describe an approach to identify tyrosine kinase substrates based on their subcellular distribution from within cells. This method uses an unnatural amino acid-modified Src homology 2 (SH2) domain that is expressed within cells and can covalently trap phosphotyrosine proteins on exposure to light. This SH2 domain-based photoprobe was targeted to cellular structures, such as the actin cytoskeleton, mitochondria, and cellular membranes, to capture tyrosine kinase substrates unique to each cellular region. We demonstrate that RhoA, one of the proteins associated with actin, can be phosphorylated on two tyrosine residues within the switch regions, suggesting that phosphorylation of these residues might modulate RhoA signaling to the actin cytoskeleton. We conclude that expression of SH2 domains within cellular compartments that are capable of covalent phototrapping can reveal the spatial organization of tyrosine kinase substrates that are likely to be important for the regulation of subcellular structures.
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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.