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- W2809347312 endingPage "964" @default.
- W2809347312 startingPage "921" @default.
- W2809347312 abstract "Protein serine/threonine phosphatases (PPPs) are ancient enzymes, with distinct types conserved across eukaryotic evolution. PPPs are segregated into types primarily on the basis of the unique interactions of PPP catalytic subunits with regulatory proteins. The resulting holoenzymes dock substrates distal to the active site to enhance specificity. This review focuses on the subunit and substrate interactions for PPP that depend on short linear motifs. Insights about these motifs from structures of holoenzymes open new opportunities for computational biology approaches to elucidate PPP networks. There is an expanding knowledge base of posttranslational modifications of PPP catalytic and regulatory subunits, as well as of their substrates, including phosphorylation, acetylation, and ubiquitination. Cross talk between these posttranslational modifications creates PPP-based signaling. Knowledge of PPP complexes, signaling clusters, as well as how PPPs communicate with each other in response to cellular signals should unlock the doors to PPP networks and signaling clouds that orchestrate and coordinate different aspects of cell physiology." @default.
- W2809347312 created "2018-06-29" @default.
- W2809347312 creator A5060827101 @default.
- W2809347312 creator A5074981380 @default.
- W2809347312 date "2018-06-20" @default.
- W2809347312 modified "2023-10-03" @default.
- W2809347312 title "Protein Serine/Threonine Phosphatases: Keys to Unlocking Regulators and Substrates" @default.
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