Ive De Smet leads the Functional Phosphoproteomics Group. To fully understand plant growth and development, we need to identify novel components and require insight in the underlying network. In this context, there is an urgent need to gain insight in protein changes on different levels, including protein-protein interactions and post-translational protein modifications. With respect to the latter, temporary and reversible phosphorylation of proteins is essential in regulating intracellular biological processes. Phosphorylation affects protein folding (conformation), protein function and the regulation of enzymatic activities, defines substrate specificity, and influences protein localization, complex formation and degradation. The mechanistic importance of phosphorylation is obvious from its major influence on various cell functions, such as signal transduction, cell division, cell differentiation, and metabolic maintenance.
As a biological model, the Functional Phosphoprotemics Group focuses on thermomorphogenesis, a process whereby plants respond to mild warm temperature conditions by increased elongation growth of organs to enhance cooling capacity. Although our understanding of temperature perception and response in plants has increased in recent years, we still know relatively little about the cellular signalling cascades that control architectural adaptations to high ambient temperatures. Arabidopsis thaliana has been proven to be an efficient model plant to study plant growth and development, but time has come to investigate signaling cascades in crop species, such as wheat and soybean, species that are currently also under investigation.
Thermomorphogenesis
Phosphatases and Kinases
In Arabidopsis and major crop species, phosphorylation is controlled by a large number of protein kinases and phosphatase complexes. However, for the majority of cytoplasmic kinases, membrane-associated receptor kinases and phosphatases unravelling physiological and developmental roles and identifying substrates remain a challenge.