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Brief Bioinform. 2013 May;14(3):344-60. doi: 10.1093/bib/bbs041. Epub 2012 Jul 31.

Systematic analysis of the Plk-mediated phosphoregulation in eukaryotes.

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1
Huazhong University of Science and Technology, Wuhan, Hubei 430074, China.

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.

KEYWORDS:

GPS; PBD; phospho-binding; phosphorylation; polo-like kinase

PMID:
22851512
DOI:
10.1093/bib/bbs041
[Indexed for MEDLINE]
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