ArticlePloS one2013
Human 14-3-3 paralogs differences uncovered by cross-talk of phosphorylation and lysine acetylation.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- 14-3-3γ Knockdown promotes matrix mineralization in human mesenchymal stromal cells.Cell death & disease · 2026Article
- Eriocheir sinensis PI3K-mediated 14-3-3ζ phosphorylation at a conserved tyrosine residue enhances ROS production to defend against Spiroplasma eriocheiris infection.Cell communication and signaling : CCS · 2026Article
- Deciphering opening mechanisms of 14-3-3 proteins.Protein science : a publication of the Protein Society · 2025Article
- YWHAG Deficiency Disrupts the EMT-Associated Network to Induce Oxidative Cell Death and Prevent Metastasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Structure of a 14-3-3ε:FOXO3aACS omega · 2022Article
- 14-3-3 Proteins are Potential Regulators of Liquid-Liquid Phase Separation.Cell biochemistry and biophysics · 2022Review
- The Highest Density of Phosphorylated Histone H1 Appeared in Prophase and Prometaphase in Parallel with Reduced H3K9me3, and HDAC1 Depletion Increased H1.2/H1.3 and H1.4 Serine 38 Phosphorylation.Life (Basel, Switzerland) · 2022Article
- Proteomic Identification of Phosphorylation-Dependent Septin 7 Interactors that Drive Dendritic Spine Formation.Frontiers in cell and developmental biology · 2022Article
- Pathways to Parkinson's disease: a spotlight on 14-3-3 proteins.NPJ Parkinson's disease · 2021Review
- Analysis of SARS-CoV-2 nucleocapsid phosphoprotein N variations in the binding site to human 14-3-3 proteins.Biochemical and biophysical research communications · 2021Article
- Involvement of the 14-3-3 Gene Family in Autism Spectrum Disorder and Schizophrenia: Genetics, Transcriptomics and Functional Analyses.Journal of clinical medicine · 2020Article
- Concatenation of 14-3-3 with partner phosphoproteins as a tool to study their interaction.Scientific reports · 2019Article
- 14-3-3/Tau Interaction and Tau Amyloidogenesis.Journal of molecular neuroscience : MN · 2019Review
- Small heat shock proteins: Simplicity meets complexity.The Journal of biological chemistry · 2019Review
- Tracking the elusive 5' exonuclease activity of Chlamydomonas reinhardtii RNase J.Plant molecular biology · 2018Article
- Article
- Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator.Structure (London, England : 1993) · 2017Article
- Bacterial co-expression of human Tau protein with protein kinase A and 14-3-3 for studies of 14-3-3/phospho-Tau interaction.PloS one · 2017Article
- Differential expression and accumulation of 14-3-3 paralogs in 3T3-L1 preadipocytes and differentiated cells.Biochemistry and biophysics reports · 2016Article
- Controllability of protein-protein interaction phosphorylation-based networks: Participation of the hub 14-3-3 protein family.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
The 14-3-3 protein family interacts with more than 700 different proteins in mammals, in part as a result of its specific phospho-serine/phospho-threonine binding activity. Upon binding to 14-3-3, the stability, subcellular localization and/or catalytic activity of the ligands are modified. Seven paralogs are strictly conserved in mammalian species. Although initially thought as redundant, the number of studies showing specialization is growing. We created a protein-protein interaction network for 14-3-3, kinases and their substrates signaling in human cells. We included information of phosphorylation, acetylation and other PTM sites, obtaining a complete representation of the 14-3-3 binding partners and their modifications. Using a computational system approach we found that networks of each 14-3-3 isoform are statistically different. It was remarkable to find that Tyr was the most phosphorylatable amino acid in domains of 14-3-3 epsilon partners. This, together with the over-representation of SH3 and Tyr_Kinase domains, suggest that epsilon could be involved in growth factors receptors signaling pathways particularly. We also found that within zeta's network, the number of acetylated partners (and the number of modify lysines) is significantly higher compared with each of the other isoforms. Our results imply previously unreported hidden differences of the 14-3-3 isoforms interaction networks. The phosphoproteome and lysine acetylome within each network revealed post-transcriptional regulation intertwining phosphorylation and lysine acetylation. A global understanding of these networks will contribute to predict what could occur when regulatory circuits become dysfunctional or are modified in response to external stimuli.
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