title: Systematic analysis of the Plk-mediated phosphoregulation in eukaryotes.
abstract: Substantial evidence has confirmed that Polo-like kinases (Plks) play a crucial role in a variety of cellular processes via phosphorylation-mediated signaling transduction. Identification of Plk phospho-binding proteins and phosphorylation substrates is fundamental for elucidating the molecular mechanisms of Plks. Here, we present an integrative approach for the analysis of Plk-specific phospho-binding and phosphorylation sites (p-sites) in proteins. From the currently available phosphoproteomic data, we predicted tens of thousands of potential Plk phospho-binding and phosphorylation sites in eukaryotes, respectively. Furthermore, statistical analysis suggested that Plk phospho-binding proteins are more closely implicated in mitosis than their phosphorylation substrates. Additional computational analysis together with in vitro and in vivo experimental assays demonstrated that human Mis18B is a novel interacting partner of Plk1, while pT14 and pS48 of Mis18B were identified as phospho-binding sites. Taken together, this systematic analysis provides a global landscape of the complexity and diversity of potential Plk-mediated phosphoregulation, and the prediction results can be helpful for further experimental investigation.
authors.affiliation: Huazhong University of Science and Technology, Wuhan, Hubei 430074, China.
authors.forename: Zexian
authors.initials: Z
authors.lastname: Liu
authors.forename: Jian
authors.initials: J
authors.lastname: Ren
authors.forename: Jun
authors.initials: J
authors.lastname: Cao
authors.forename: Jiang
authors.initials: J
authors.lastname: He
authors.forename: Xuebiao
authors.initials: X
authors.lastname: Yao
authors.forename: Changjiang
authors.initials: C
authors.lastname: Jin
authors.forename: Yu
authors.initials: Y
authors.lastname: Xue
mesh_terms: D000465:Algorithms; D018797:Cell Cycle Proteins / Q000378:metabolism / Q000502:physiology*; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism; D005057:Eukaryotic Cells; D006801:Humans; D008954:Models, Biological; D010766:Phosphorylation; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism / Q000502:physiology*; D011518:Proto-Oncogene Proteins / Q000378:metabolism / Q000502:physiology*; D000097869:Polo-Like Kinase 1
chemical_list: D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins; D000097869:Polo-Like Kinase 1; C517146:OIP5 protein, human