Protein Kinase D2 recruitment to the trans-Golgi network requires the first and second cysteine-rich zinc finger domains

Introduction: Protein Kinase D2 (PKD2) is a member of the PKD family of serine/threonine kinases, which in turn belongs to the CAMK family. PKDs are activated either directly via phorbol esters or indirectly by various mechanisms including G protein-coupled receptors. These kinases are implicated in various biological processes such as proliferation, apoptosis and regulation of Golgi function. PKDs have an N-terminal regulatory domain comprising two cysteine-rich zinc finger domains (C1a and C1b) and a pleckstrin homology domain, and a C-terminal kinase domain. These individual domains regulate the localization…