ArticleACS chemical biology2017
Site-Specific Phosphorylation of PSD-95 PDZ Domains Reveals Fine-Tuned Regulation of Protein-Protein Interactions.
Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 45 citations in OpenAlex.
- Exploration of schizophrenia-related behavioral and molecular abnormalities in a mutant mouse model with a mutation in the TVV motif of the ErbB4 gene.Molecular brain · 2025Article
- Rational Design of Pyrido[3,2-JACS Au · 2024Article
- Genetic Encoding of Phosphorylated Amino Acids into Proteins.Chemical reviews · 2024Review
- "NO" Time in Fear Response: Possible Implication of Nitric-Oxide-Related Mechanisms in PTSD.Molecules (Basel, Switzerland) · 2023Review
- Human Serine Racemase Weakly Binds the Third PDZ Domain of PSD-95.International journal of molecular sciences · 2022Article
- Neurodevelopmental Disorders Associated with PSD-95 and Its Interaction Partners.International journal of molecular sciences · 2022Review
- Bidirectional protein-protein interactions control liquid-liquid phase separation of PSD-95 and its interaction partners.iScience · 2022Article
- PSD-95: An Effective Target for Stroke Therapy Using Neuroprotective Peptides.International journal of molecular sciences · 2021Review
- Site-specific phosphorylation of PSD-95 dynamically regulates the postsynaptic density as observed by phase separation.iScience · 2021Article
- Zinc-chelating postsynaptic density-95 N-terminus impairs its palmitoyl modification.Protein science : a publication of the Protein Society · 2021Article
- Dynamic bi-directional phosphorylation events associated with the reciprocal regulation of synapses during homeostatic up- and down-scaling.Cell reports · 2021Article
- Functional cross-talk between phosphorylation and disease-causing mutations in the cardiac sodium channel NaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Molecular Details of a Coupled Binding and Folding Reaction between the Amyloid Precursor Protein and a Folded Domain.ACS chemical biology · 2021Article
- Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Noncanonical Sequences Involving NHERF1 Interaction with NPT2A Govern Hormone-Regulated Phosphate Transport: Binding Outside the Box.International journal of molecular sciences · 2021Review
- Phosphorylation-induced changes in the PDZ domain of Dishevelled 3.Scientific reports · 2021Article
- Dynamic Control of Signaling by Phosphorylation of PDZ Binding Motifs.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Deciphering protein post-translational modifications using chemical biology tools.Nature reviews. Chemistry · 2020Review
- The Conformational Plasticity Vista of PDZ Domains.Life (Basel, Switzerland) · 2020Review
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
The postsynaptic density protein of 95 kDa (PSD-95) is a key scaffolding protein that controls signaling at synapses in the brain through interactions of its PDZ domains with the C-termini of receptors, ion channels, and enzymes. PSD-95 is highly regulated by phosphorylation. To explore the effect of phosphorylation on PSD-95, we used semisynthetic strategies to introduce phosphorylated amino acids at four positions within the PDZ domains and examined the effects on interactions with a large set of binding partners. We observed complex effects on affinity. Most notably, phosphorylation at Y397 induced a significant increase in affinity for stargazin, as confirmed by NMR and single molecule FRET. Additionally, we compared the effects of phosphorylation to phosphomimetic mutations, which revealed that phosphomimetics are ineffective substitutes for tyrosine phosphorylation. Our strategy to generate site-specifically phosphorylated PDZ domains provides a detailed understanding of the role of phosphorylation in the regulation of PSD-95 interactions.
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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.