UC San Diego

Protein kinase C (PKC) is an archetypal mediator of cellular signaling. PKC consists of 10 Ser/Thr kinases that participate in a wide range of cellular processes, including proliferation, apoptosis, learning and memory, and cell migration. PKC signaling is controlled by lipid second messengers and protein scaffolding. For proper cellular PKC signaling, location and timing of activation are critical. Aberrant PKC signaling is known to occur in disease states, notably cancer. The goal of this thesis is to examine how spatial and temoral specificity are achieved in cellular PKC signaling, and how this regulation is altered in cancer. Understanding the nuances of PKC regulation in cells and mis-regulation in disease will undoubtedly inform efforts to therapeutically target this enzyme family