Role of the kinase activation loop on protein kinase C θ activity and intracellular localisation
Open Access
- 8 October 2003
- journal article
- Published by Wiley in FEBS Letters
- Vol. 554 (1-2) , 35-40
- https://doi.org/10.1016/s0014-5793(03)01073-1
Abstract
Multiple protein kinase C (PKC) θ species, identified in an erythroleukaemia cell line, have been characterised in terms of their molecular properties and intracellular distribution. PKCθs localised in the detergent‐soluble cell fraction have an M r of 76 kDa (θ‐76) and contain Thr538 or pThr538 in the kinase activation loop. In contrast, PKCθs localised in the Golgi complex have an M r of 85 kDa (θ‐85) and, although unphosphorylated at Thr538, are catalytically active. Strikingly, only θ‐76 species which are unphosphorylated at Thr538 can undergo autocatalytic conversion to θ‐85. Moreover, a Thr538→Ala PKCθ mutant is constitutively localised in the Golgi complex, confirming that changes in the phosphorylation state of this residue play a pivotal role in the overall control of catalytic properties and localisation of this kinase.Keywords
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