Capturing conformational transitions of full-length PDK1 that dictate kinase substrate selectivity

Sci Signal. 2023 Jun 13;16(789):eadh5114. doi: 10.1126/scisignal.adh5114. Epub 2023 Jun 13.

Abstract

PDK1 is a constitutively active master kinase that can phosphorylate and activate as many as 24 enzymes, all belonging to the AGC family of serine-threonine protein kinases. In this issue of Science Signaling, Sacerdoti et al. uncover how allosteric communication between different functional domains directs the selectivity of PDK1 toward particular subsets of substrates.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Protein Serine-Threonine Kinases* / genetics
  • Signal Transduction*

Substances

  • Protein Serine-Threonine Kinases