ArticlePacific Symposium on Biocomputing. Pacific Symposium on Biocomputing2009
High throughput interaction data reveals degree conservation of hub proteins.
Article in Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Correlated Evolution Drives Structural Convergence of Interacting Proteins.Journal of molecular evolution · 2026Article
- Topsy-Turvy: integrating a global view into sequence-based PPI prediction.Bioinformatics (Oxford, England) · 2022Article
- Molecular dysexpression in gastric cancer revealed by integrated analysis of transcriptome data.Oncology letters · 2017Article
- What evidence is there for the homology of protein-protein interactions?PLoS computational biology · 2012Article
- Biological interaction networks are conserved at the module level.BMC systems biology · 2011Article
- Connectedness of PPI network neighborhoods identifies regulatory hub proteins.Bioinformatics (Oxford, England) · 2011Article
- FEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.PloS one · 2011Article
- Deciphering peculiar protein-protein interacting modules in Deinococcus radiodurans.Biology direct · 2009Article
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3 authors.
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Abstract
Research in model organisms relies on unspoken assumptions about the conservation of protein-protein interactions across species, yet several analyses suggest such conservation is limited. Fortunately, for many purposes the crucial issue is not global conservation of interactions, but preferential conservation of functionally important ones. An observed bias towards essentiality in highly-connected proteins implies the functional importance of such "hubs". We therefore define the notion of degree-conservation and demonstrate that hubs are preferentially degree-conserved. We show that a protein is more likely to be a hub if it has a high-degree ortholog, and that once a protein becomes a hub, it tends to remain so. We also identify a positive correlation between the average degree of a protein and the conservation of its interaction partners, and we find that the conservation of individual hub interactions is surprisingly high. Our work has important implications for prediction of protein function, computational inference of PPIs, and interpretation of data from model organisms.
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