Protein kinases, from B to C

A. J. Cameron, M. De Rycker, V. Calleja, D. Alcor, S. Kjaer, B. Kostelecky, A. Saurin, A. Faisal, M. Laguerre, B. A. Hemmings, N. McDonald, B. Larijani, P. J. Parker

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

The PKB (protein kinase B) and PKC (protein kinase C) families display highly related catalytic domains that require a largely conserved series of phosphorylations for the expression of their optimum activities. However, in cells, the dynamics of these modifications are quite distinct. Based on experimental evidence, it is argued that the underlying mechanisms determining these divergent behaviours relate to the very different manner in which their variant regulatory domains interact with their respective catalytic domains. It is concluded that the distinct behaviours of PKB and PKC proteins are defined by the typical ground states of these proteins.

Original languageEnglish
Pages (from-to)1013-1017
Number of pages5
JournalBiochemical Society Transactions
Volume35
Issue number5
DOIs
Publication statusPublished - 1 Nov 2007

Keywords

  • Phosphoinositide-dependent kinase 1 (PDK1)
  • Phosphorylation
  • Pleckstrin homology domain (PH domain)
  • Protein kinase B (PKB)
  • Protein kinase C (PKC)
  • Protein serine/threonine kinase

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