Evidence for a Minimal Eukaryotic Phosphoproteome?
2007

Evidence for a Minimal Eukaryotic Phosphoproteome

publication Evidence: moderate

Author Information

Author(s): Diks Sander H., Parikh Kaushal, van der Sijde Marijke, Joore Jos, Ritsema Tita, Peppelenbosch Maikel P.

Primary Institution: University Medical Center Groningen, University of Groningen

Hypothesis

The study investigates whether a minimal set of kinase substrates exists across divergent eukaryotic species.

Conclusion

The results indicate that a limited common substrate space for kinases exists in eukaryotes, suggesting the presence of a set of kinase substrates in an ancestral eukaryote that has remained constant.

Supporting Evidence

  • The study identified a set of 128 substrates that are phosphorylated by cell lysates from various eukaryotic sources.
  • Phosphorylation profiles showed significant overlap among lysates from different eukaryotic origins.
  • The findings suggest that the minimal eukaryotic phosphoproteome is essential for maintaining cell homeostasis.

Takeaway

Scientists found that many different types of cells can use the same basic building blocks to do their jobs, showing that these building blocks have been around for a long time.

Methodology

The study used peptide arrays to analyze the phosphorylation of substrates by cell lysates from various eukaryotic species.

Potential Biases

The peptide array used was strongly biased towards mammalian sequences, which may affect the generalizability of the findings.

Limitations

The study is biased towards mammalian peptide sequences and may not fully represent the diversity of kinase substrates in non-mammalian species.

Statistical Information

P-Value

p<0.01

Statistical Significance

p<0.01

Digital Object Identifier (DOI)

10.1371/journal.pone.0000777

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