The origins and evolution of ubiquitination sites

Molecular BioSystems
Tzachi HagaiYaakov Levy

Abstract

Protein ubiquitination is central to the regulation of various pathways in eukaryotes. The process of ubiquitination and its cellular outcome were investigated in hundreds of proteins to date. Despite this, the evolution of this regulatory mechanism has not yet been addressed comprehensively. Here, we quantify the rates of evolutionary changes of ubiquitination and SUMOylation (Small Ubiquitin-like MOdifier) sites. We estimate the time at which they first appeared, and compare them to acetylation and phosphorylation sites and to unmodified residues. We observe that the various modification sites studied exhibit similar rates. Mammalian ubiquitination sites are weakly more conserved than unmodified lysine residues, and a higher degree of relative conservation is observed when analyzing bona fide ubiquitination sites. Various reasons can be proposed for the limited level of excess conservation of ubiquitination, including shifts in locations of the sites, the presence of alternative sites, and changes in the regulatory pathways. We observe that disappearance of sites may be compensated by the presence of a lysine residue in close proximity, which is significant when compared to evolutionary patterns of unmodified lysine residues,...Continue Reading

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Citations

Nov 20, 2012·BMC Bioinformatics·Dong Seon Kim, Yoonsoo Hahn
Feb 26, 2014·The Journal of Cell Biology·Takumi MikawaHiroshi Kondoh
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Jul 18, 2018·International Journal of Molecular Medicine·Dongbin ParkYoonsoo Hahn
Jul 13, 2014·The Journal of Biological Chemistry·Etienne KhouryStéphane A Laporte

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