title: Protein disorder in the centrosome correlates with complexity in cell types number.
abstract: Here we study the properties and the evolution of proteins that constitute the Centrosome, the complex molecular assembly that regulates the division and differentiation of animal cells. We found that centrosomal proteins are predicted to be significantly enriched in disordered and coiled-coil regions, more phosphorylated and longer than control proteins of the same organism. Interestingly, the ratio of these properties in centrosomal and control proteins tends to increase with the number of cell-types. We reconstructed indels evolution, finding that indels significantly increase disorder in both centrosomal and control proteins, at a rate that is typically larger along branches associated with a large growth in cell-types number, and larger for centrosomal than for control proteins. Substitutions show a similar trend for coiled-coil, but they contribute less to the evolution of disorder. Our results suggest that the increase in cell-types number in animal evolution is correlated with the gain of disordered and coiled-coil regions in centrosomal proteins, establishing a connection between organism and molecular complexity. We argue that the structural plasticity conferred to the Centrosome by disordered regions and phosphorylation plays an important role in its mechanical properties and its regulation in space and time.
authors.affiliation: Centro de Biología Molecular Severo Ochoa, (CSIC-UAM), Madrid, Spain.
authors.forename: G S
authors.initials: GS
authors.lastname: Nido
authors.forename: R
authors.initials: R
authors.lastname: Méndez
authors.forename: A
authors.initials: A
authors.lastname: Pascual-García
authors.forename: D
authors.initials: D
authors.lastname: Abia
authors.forename: U
authors.initials: U
authors.lastname: Bastolla
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002452:Cell Count; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism*; D018385:Centrosome / Q000378:metabolism*; D019143:Evolution, Molecular; D005580:Fossils; D006801:Humans; D054643:INDEL Mutation / Q000235:genetics; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010802:Phylogeny; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D013997:Time Factors
chemical_list: D018797:Cell Cycle Proteins