The serine/threonine kinase protein kinase D (PKD) was first described in 1994. Due to some homology in its kinase domain, its ability to bind the lipid diacylglycerol (DAG), and its responsiveness to phorbol ester, PKD was originally classified as a member of the protein kinase C (PKC) family (Johannes et al. 1994). Later it became evident that PKD represents an own group of kinases more closely related to the calcium/calmodulin-regulated (Cam) kinases (Manning et al. 2002). Initially, the PKD field focused on determining the functions of the structural elements and domains of PKD1 as well as the activation mechanisms for this kinase. With the identification of the PKD phosphorylation motif (Hutti et al. 2004) and the subsequent generation of a substrate-specific antibody (Döppler et al. 2005), optimal conditions were provided for the discovery of PKD substrates. This led to an increasing wealth of information...
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