Evidence for a minimal eukaryotic phosphoproteome?

Sander H. Diks*, Kaushal Parikh, Marijke van der Sijde, Jos Joore, Tita Ritsema, Maikel P. Peppelenbosch

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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Reversible phosphorylation catalysed by kinases is probably the most important regulatory mechanism in eukaryotes. 

Methodology/Principal Findings:

We studied the in vitro phosphorylation of peptide arrays exhibiting the majority of PhosphoBase-deposited protein sequences, by factors in cell lysates from representatives of various branches of the eukaryotic species. We derived a set of substrates from the PhosphoBase whose phosphorylation by cellular extracts is common to the divergent members of different kingdoms and thus may be considered a minimal eukaryotic phosphoproteome. The protein kinases (or kinome) responsible for phosphorylation of these substrates are involved in a variety of processes such as transcription, translation, and cytoskeletal reorganisation.


These results indicate that the divergence in eukaryotic kinases is not reflected at the level of substrate phosphorylation, revealing the presence of a limited common substrate space for kinases in eukaryotes and suggests the presence of a set of kinase substrates and regulatory mechanisms in an ancestral eukaryote that has since remained constant in eukaryotic life.

Original languageEnglish
Article numbere777
JournalPLoS ONE
Issue number8
Publication statusPublished - 22 Aug 2007
Externally publishedYes

Bibliographical note

This work was supported in part by grants from the regional
programme of innovative actions in Groningen (IAG) and Top Institute Pharma
(TI Pharma). SHD is supported by a Casimir fellowship funded by the Netherlands
Organisation for Scientific Research (NWO).


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