ArticleMolecular & cellular proteomics : MCP2009
In silico analysis of phosphoproteome data suggests a rich-get-richer process of phosphosite accumulation over evolution.
Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 32 citations in OpenAlex.
- Phosphorylation and Pin1 binding to the LIC1 subunit selectively regulate mitotic dynein functions.The Journal of cell biology · 2021Article
- Role ofPhysiological reviews · 2021Review
- Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2020Article
- Phosphoproteomics ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Proteomic profiling and functional characterization of post-translational modifications of the fission yeast RNA exosome.Nucleic acids research · 2018Article
- Landscape of the complete RNA chemical modifications in the human 80S ribosome.Nucleic acids research · 2018Article
- Gene Expression Order Attributed to Genome Reduction and the Steady Cellular State inFrontiers in microbiology · 2018Article
- Crosstalk between signaling pathways provided by single and multiple protein phosphorylation sites.Journal of molecular biology · 2015Article
- Ubiquitination site preferences in anaphase promoting complex/cyclosome (APC/C) substrates.Open biology · 2013Article
- Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse.Molecular & cellular proteomics : MCP · 2012Article
- Evaluation and properties of the budding yeast phosphoproteome.Molecular & cellular proteomics : MCP · 2012Article
- Human Protein Reference Database and Human Proteinpedia as resources for phosphoproteome analysis.Molecular bioSystems · 2012Review
- Phosphorylation in protein-protein binding: effect on stability and function.Structure (London, England : 1993) · 2011Article
- Integrative features of the yeast phosphoproteome and protein-protein interaction map.PLoS computational biology · 2011Article
- Proteome-wide survey of phosphorylation patterns affected by nuclear DNA polymorphisms in Arabidopsis thaliana.BMC genomics · 2010Article
- Towards the systematic discovery of signal transduction networks using phosphorylation dynamics data.BMC bioinformatics · 2010Article
- Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data.Biology direct · 2010Article
- Phosphoproteomics by mass spectrometry: insights, implications, applications and limitations.Expert review of proteomics · 2009Article
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5 authors at 2 institutions in 1 country.
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Abstract
Recent phosphoproteome analyses using mass spectrometry-based technologies have provided new insights into the extensive presence of protein phosphorylation in various species and have raised the interesting question of how this protein modification was gained evolutionarily on such a large scale. We investigated this issue by using human and mouse phosphoproteome data. We initially found that phosphoproteins followed a power-law distribution with regard to their number of phosphosites: most of the proteins included only a few phosphosites, but some included dozens of phosphosites. The power-law distribution, unlike more commonly observed distributions such as normal and log-normal distributions, is considered by the field of complex systems science to be produced by a specific rich-get-richer process called preferential attachment growth. Therefore, we explored the factors that may have promoted the rich-get-richer process during phosphosite evolution. We conducted a bioinformatics analysis to evaluate the relationship of amino acid sequences of phosphoproteins with the positions of phosphosites and found an overconcentration of phosphosites in specific regions of protein surfaces and implications that in many phosphoproteins these clusters of phosphosites are activated simultaneously. Multiple phosphosites concentrated in limited spaces on phosphoprotein surfaces may therefore function biologically as cooperative modules that are resistant to selective pressures during phosphoprotein evolution. We therefore proposed a hypothetical model by which the modularization of multiple phosphosites has been resistant to natural selection and has driven the rich-get-richer process of the evolutionary growth of phosphosite numbers.
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