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 Mr 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 Thr 538, 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.
| Lingua originale | Inglese |
|---|---|
| pagine (da-a) | 35-40 |
| Numero di pagine | 6 |
| Rivista | FEBS Letters |
| Volume | 554 |
| Numero di pubblicazione | 1-2 |
| DOI | |
| Stato di pubblicazione | Pubblicato - 6 nov 2003 |