We show that protein kinase C (PKC) h localized at the Golgi complex is partially conjugated to monoubiquitin. Using the inactive T538A and activable T538E mutants of PKCh, we demonstrate that the presence of an uncharged residue at the 538 position of the activation loop favors both association with the Golgi and monoubiquitination of the kinase. Moreover, the inactive PKCh does not translocate from the Golgi in response to a short-term cell stimulation with a phorbol ester and is subjected to different proteolytic degradation pathways compared to the activable cytosolic kinase. These findings highlight the role of T538 as a critical determinant to address the activable and the inactive PKCh molecules to different intracellular compartments and to specific post-transductional modifications. The functional relevance of these observations is supported by the impaired cell division observed in phenotypes expressing high levels of the inactive PKCh. 2008 Elsevier Inc. All rights reserved.
|Titolo:||Functional role of the charge at the T538 residue in the control of protein kinase Ctheta|
|Data di pubblicazione:||2009|
|Appare nelle tipologie:||01.01 - Articolo su rivista|