Protein kinases, from B to C

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

doi:10.1042/bst0351013

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Journal article

Protein kinases, from B to C

Cameron, A.J. Protein Phosphorylation Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
De Rycker, M. Protein Phosphorylation Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
Calleja, V. Cell Biophysics Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
Alcor, D. Cell Biophysics Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
Kjaer, S. Structural Biology Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
Kostelecky, B. Structural Biology Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
Saurin, A. Protein Phosphorylation Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
Faisal, A. Protein Phosphorylation Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
Laguerre, M. Institut Européen de Chimie et Biologie, Pessac Cedex, France
Hemmings, B.A. Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH 4058 Basel, Switzerland
McDonald, N. Structural Biology Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
Larijani, B. Cell Biophysics Lab, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
Parker, P.J. Head of the Division of Cancer Studies KCL, Section of Cancer Cell Biology and Imaging, New Hunt's House, Guy's Hospital, St Thomas Street, London SE1 1UL, U.K.

2007-10-25

Published in:

Biochemical Society Transactions. - Portland Press Ltd.. - 2007, vol. 35, no. 5, p. 1013-1017

Biochemistry

English 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.

Language

English

Open access status

green

Identifiers

DOI 10.1042/bst0351013
ISSN 0300-5127

Persistent URL

https://sonar.ch/global/documents/5841

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