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Evolving Cell Signals

Protein phosphorylation has emerged as a ubiquitous regulatory switch in cell signaling networks. Improved methods to purify and characterize phosphopeptides have led to an explosion of phosphorylation site data, and we can now explore how protein phosphorylation evolved. This perspective discusses a report by Tan et al. showing that tyrosine residues (which can be phosphorylated) have been selectively lost through metazoan evolution, as well as a report by Holt et al., who show that most phosphorylation sites shift position in rapidly evolving, disordered regions of proteins.

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Resource Type: Journal article/Issue, Illustration
Audience Level: Undergraduate lower division 13-14, Undergraduate upper division 15-16, Graduate, Professional (degree program), Continuing education

Author and Copyright

Authors and Editors: Mark Collins of Proteomic Mass Spectrometry Group, The Wellcome Trust Sanger Institute
Publisher: SCIENCE
Format: text/html
Copyright and other restrictions: Yes
Cost: No


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