How Do Protein Kinases Take a Selfie (Autophosphorylate)?

Jonah Beenstock, Navit Mooshayef, David Engelberg

Research output: Contribution to journalReview articlepeer-review


Eukaryotic protein kinases (EPKs) control most biological processes and play central roles in many human diseases. To become catalytically active, EPKs undergo conversion from an inactive to an active conformation, an event that depends upon phosphorylation of their activation loop. Intriguingly, EPKs can use their own catalytic activity to achieve this critical phosphorylation. In other words, paradoxically, EPKs catalyze autophosphorylation when supposedly in their inactive state. This indicates the existence of another important conformation that specifically permits autophosphorylation at the activation loop, which in turn imposes adoption of the active conformation. This can be considered a prone-to-autophosphorylate conformation. Recent findings suggest that in prone-to-autophosphorylate conformations catalytic motifs are aligned allosterically, by dimerization or by regulators, and support autophosphorylation in cis or trans.

Original languageEnglish
Pages (from-to)938-953
Number of pages16
JournalTrends in Biochemical Sciences
Issue number11
StatePublished - 1 Nov 2016


  • allostery
  • autophosphorylation
  • dimerization
  • protein kinase.

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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