ArticleMolecular bioSystems2013
Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: analysis of human protein complexes.
Article in Molecular bioSystems, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- STYXL1 regulates CCT complex assembly and flagellar tubulin folding in sperm formation.Nature communications · 2024Article
- Phosphorylated Proteins from Serum: A Promising Potential Diagnostic Biomarker of Cancer.International journal of molecular sciences · 2022Review
- Dynamics of huntingtin protein interactions in the striatum identifies candidate modifiers of Huntington disease.Cell systems · 2022Article
- The auto-inhibition mechanism of transcription factor Ets-1 induced by phosphorylation on the intrinsically disordered region.Computational and structural biotechnology journal · 2022Article
- Influence of the Season and Region Factor on Phosphoproteome of Stallion Epididymal Sperm.Animals : an open access journal from MDPI · 2021Article
- Identification of Phosphorylated Calpain 3 in Rat Brain Mitochondria under mPTP Opening.International journal of molecular sciences · 2021Article
- Article
- Phosphorylation regulates the binding of intrinsically disordered proteins via a flexible conformation selection mechanism.Communications chemistry · 2020Article
- PEBP1/RKIP behavior: a mirror of actin-membrane organization.Cellular and molecular life sciences : CMLS · 2020Article
- Endogenous AT1 receptor-protein kinase C activity in the hypothalamus augments glutamatergic input and sympathetic outflow in hypertension.The Journal of physiology · 2019Article
- Article
- Caspase-9 CARD : core domain interactions require a properly formed active site.The Biochemical journal · 2018Article
- Computational modeling suggests impaired interactions between NKX2.5 and GATA4 in individuals carrying a novel pathogenic D16N NKX2.5 mutation.Oncotarget · 2018Article
- Article
- The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (Review).International journal of molecular medicine · 2017Review
- Effect of Phosphorylation on a Human-like Osteopontin Peptide.Biophysical journal · 2017Article
- Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics.Journal of molecular biology · 2017Article
- Prioritizing functional phosphorylation sites based on multiple feature integration.Scientific reports · 2016Article
- Reads meet rotamers: structural biology in the age of deep sequencing.Current opinion in structural biology · 2015Review
- Evolution of the highly networked deubiquitinating enzymes USP4, USP15, and USP11.BMC evolutionary biology · 2015Article
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Authors and funding
5 authors.
Funding
Abstract
Phosphorylation offers a dynamic way to regulate protein activity, subcellular localization, and stability. The majority of signaling pathways involve an extensive set of protein-protein interactions, and phosphorylation is widely used to regulate protein-protein binding by affecting the stability, kinetics and specificity of interactions. Previously it was found that phosphorylation sites tend to be located on protein-protein binding interfaces and may orthosterically modulate the strength of interactions. Here we studied the effect of phosphorylation on protein binding in relation to intrinsic disorder for different types of human protein complexes with known structure of the binding interface. Our results suggest that the processes of phosphorylation, binding and disorder-order transitions are coupled to each other, with about one quarter of all disordered interface Ser/Thr/Tyr sites being phosphorylated. Namely, residue site disorder and interfacial states significantly affect the phosphorylation of serine and to a lesser extent of threonine. Tyrosine phosphorylation might not be directly associated with binding through disorder, and is often observed in ordered interface regions which are not predicted to be disordered in the unbound state. We analyze possible mechanisms of how phosphorylation might regulate protein-protein binding via intrinsic disorder, and specifically focus on how phosphorylation could prevent disorder-order transitions upon binding.
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