Acute regulation of PDK1 by a complex interplay of molecular switches

Veronique Calleja, Michel Laguerre, Gloria de Las Heras-Martinez, Peter J Parker, Jose Requejo-Isidro, Banafshé Larijani

Research output: Contribution to journalReview articlepeer-review

24 Citations (SciVal)


Phosphoinositide-dependent kinase 1 (PDK1) is the master regulator of at least 23 other AGC kinases whose downstream signalling has often been implicated in various diseases and in particular in cancer. Therefore there has been great interest in determining how PDK1 is controlled and how it regulates its substrates spatially and temporally. The understanding of these mechanisms could offer new possibilities for therapeutic intervention. Over the years, a more comprehensive view of the mechanisms involved in the regulation of PDK1 has emerged and these comprise serine/threonine as well as tyrosine phosphorylation, subcellular localization, regulator binding and conformation status. In the present review, we discuss how various molecular mechanisms are together responsible for the conformational regulation behind the activation of PDK1 in cells.

Original languageEnglish
Pages (from-to)1435-40
Number of pages6
JournalBiochemical Society Transactions
Issue number5
Publication statusPublished - Oct 2014


  • 3-Phosphoinositide-Dependent Protein Kinases/chemistry
  • Animals
  • Dimerization
  • Enzyme Activation
  • Humans
  • Ligands
  • Models, Molecular
  • Neoplasm Proteins/chemistry
  • Phosphorylation
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Protein Transport
  • Serine/metabolism
  • Signal Transduction
  • Threonine/metabolism
  • Tyrosine/metabolism


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