Positive Selection of Tyrosine Loss in Metazoan Evolution

Author:

Tan Chris Soon Heng123,Pasculescu Adrian1,Lim Wendell A.4,Pawson Tony12,Bader Gary D.123,Linding Rune5

Affiliation:

1. Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto M5G 1X5, Canada.

2. Department of Molecular Genetics, University of Toronto, Toronto M5S 1A8, Canada.

3. Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto M5S 3E1, Canada.

4. Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA.

5. Cellular and Molecular Logic Team, Section of Cell and Molecular Biology, The Institute of Cancer Research (ICR), London, SW3 6JB, UK.

Abstract

Cataloging Kinase Targets Protein phosphorylation is a central mechanism in the control of many biological processes (see the Perspective by Collins ). It remains a challenge to determine the complete range of substrates and phosphorylation sites altered by a kinase like cyclin-dependent kinase 1 (Cdk1), which controls cell division in yeast. Holt et al. (p. 1682 ) engineered a strain of yeast to express a modified Cdk1 molecule that could be inhibited by a specific small-molecule inhibitor. The range of Cdk1-dependent phosphorylation was assessed by quantitative mass spectrometry, which revealed many previously uncharacterized substrates for Cdk1. In addition to phosphorylation on serine and threonine residues, which appears to be evolutionarily ancient, tyrosine phosphorylation occurs primarily in multicellular organisms. Tan et al. (p. 1686 , published online 9 July) compared the overall presence of tyrosine residues in human proteins (which are frequently phosphorylated) and in yeast proteins (which are not). Loss of tyrosine residues has occurred during evolution, presumably to reduce adventitious tyrosine phosphorylation.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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