FOR 964 - Central Project 1 - Calcium signaling via protein phosphorylation in plant model cell types during environmental stress adaption (FOR 964-TP Z1)

Basic data for this project

Description

Transient increases in cytosolic calcium ([Ca2+]cyt) are integral parts of multiple signaling pathways. One of the key questions in signal transduction therefore is how such a ubiquitous second messenger can control the specificity of diverse cellular responses. Elements that could contribute to encoding specificity are the spatio-temporal characteristics of so-called Ca2+-signatures determined by the involvement of different subcellular Ca2+-stores combined with the kinetics of the respective in- and efflux transporters as well as the differential activation of Ca2+-dependent protein kinases as the decoding elements. Remarkably, recent results suggest that Ca2+-dependent protein kinases are not only involved in decoding but also in encoding calcium-signals as they regulate membrane transporters directly or indirectly involved in shaping Ca2+-signatures. However, experimental evidence supporting this conceptual framework is limited and the proposed Research Unit therefore combines experts in the fields of Ca2+-dependent phosphorylation and membrane transport to achieve a detailed and integrative understanding of calcium signaling. We will focus our efforts on a comprehensive and comparative analysis of calcium signaling during abiotic stress in two model cell types, stomata and root hairs, deploying state-of-the-art techniques including live-cell imaging, electrophysiology and phosphoproteomics.The specific aims of the proposed Research Unit are to: identify and characterize the components and mechanisms leading to localized and transient changes in (sub-)cellular Ca2+ concentration elucidate the contribution of different sub-cellular compartments as sources and reservoirs for Ca2+ signaling investigate the function and regulation of Ca2+-dependent kinases and their interactions with other signaling components to identify and characterize the targets of Ca2+-dependent protein kinases