Ontology highlight
ABSTRACT:
SUBMITTER: Hauge C
PROVIDER: S-EPMC1864980 | biostudies-literature | 2007 May
REPOSITORIES: biostudies-literature
Hauge Camilla C Antal Torben L TL Hirschberg Daniel D Doehn Ulrik U Thorup Katrine K Idrissova Leila L Hansen Klaus K Jensen Ole N ON Jørgensen Thomas J TJ Biondi Ricardo M RM Frödin Morten M
The EMBO journal 20070419 9
The growth factor/insulin-stimulated AGC kinases share an activation mechanism based on three phosphorylation sites. Of these, only the role of the activation loop phosphate in the kinase domain and the hydrophobic motif (HM) phosphate in a C-terminal tail region are well characterized. We investigated the role of the third, so-called turn motif phosphate, also located in the tail, in the AGC kinases PKB, S6K, RSK, MSK, PRK and PKC. We report cooperative action of the HM phosphate and the turn m ...[more]