Van Damme Daniel

Van Damme Daniel - Group leader

My research career started in 2001 at Ghent University. I initially focused on the regulation of cytokinesis, more specifically, how plants determine quite early during the cell cycle, where the new cell wall that divides both daughter cells will be constructed. The initial fluorescence-based localization screen that I performed in tobacco BY-2 cells revealed several new proteins that were specifically recruited to the forming cell plate. We are now 20 years later, yet one of those proteins that I initially identified then is still the cornerstone of my current research.
After my PhD in 2006, I joined the newly established lab of Eugenia Russinova at the Department of Plant Systems Biology (PSB VIB/UGent) as a postdoctoral fellow of the Research Foundation of Flanders (FWO), working on the role of the alpha-type aurora kinases in cell plate orientation during the first asymmetric divisions leading to the formation of lateral root primordia. I consider myself very lucky that already at a very early point in my career, I was allowed to independently pursue my own project. My longstanding collaboration with the group of Geert De Jaeger (PSB VIB/UGent) was initiated during my second postdoctoral term as an FWO fellow. Together, we embarked on a joint PhD project that combined interactomics via tandem affinity purification on a set of bait proteins from my original localization screen, with live cell imaging in planta.  The results from this collaboration allowed me to create my niche research that continues until today as it was then that we discovered the existence of the TPLATE complex and its crucial role in plant endocytosis.
After my second postdoctoral term, I successfully applied for the position as expert scientist for live cell imaging that was opened at the Center for Plant Systems Biology. This position served to provide expertise, experimental design, acquisition and maintenance as well as practical assistance to the researchers at PSB for all aspects of fluorescence-based live cell imaging. At the same time, it provided me with the necessary time to finalize the dissection of the role of our newly discovered endocytic complex. I am still very proud that the discovery of the existence of this evolutionary ancient multi-protein complex was made in plants first, albeit only a few months in advance of the publication characterizing this complex in slime moulds.
The structural and functional elucidation of the process of endocytosis in plants was the topic of my LS3 ERC Consolidator Grant, which I obtained in 2016. That year, I also became associate professor at Ghent University, in the Department of Plant Biotechnology and Bioinformatics as well as Principle Investigator of advanced live cell imaging group at VIB. In 2018, I became full professor.
My current research focuses on the mechanistic regulation of how endocytosis modulates cellular communication by controlling the abundance of receptors and channels in its plasma membrane. We do this by combining interactomics as well as structural and cell biology on the endocytic machinery. Next to this, together with my microscopy expert, Evelien Mylle, I continue to provide assistance and maintenance of the light microscopy infrastructure of the Center.
Throughout my research career, and quite obvious from my publication record, I have always shared my initial data with the research community early on and actively reached out to other groups to pursue research collaborations. This approach allowed me to establish a broad and international network of colleagues to fall back on and the heterosis that is generated from the combined efforts of multiple labs significantly contributed to the quality of my research.
 

C9orf72 ALS shows muted microglial response

ALS driven by the C9orf72 hexanucleotide repeat expansion shows a fundamentally different glial response than sporadic ALS, despite near-identical clinical presentation. The findings by the team of Renzo Mancuso at the VIB-UAntwerp Center for Molecular Neurology, together with Philip Van Damme at KU Leuven/UZ Leuven, and the Van Den Bosch lab at the VIB-KU Leuven Center for Biology of Disease Research, were published in Nature Neuroscience.

Microscopy Imaging tools at PSB

Microscopy Imaging tools at PSB

 

PSB researchers are actively involved in generating tools to allow real-time visualization of plants under conditions that disturb specific processes. Examples are the use of microfluidics setups to monitor the effect of chemical compounds as well as the effect of altered temperature, on cellular dynamics. 

Temperature-modulated live cell imaging

Temperature-modulated live cell imaging.

Dynamic imaging of fast-occurring processes is hampered by the fact that the signal/noise ratio of a fluorescent image is inversely related to the exposure time. The exposure time in turn limits the imaging speed and thereby the temporal resolution. We are increasing the temporal resolution of live-cell imaging plant samples by modulating the temperature of the samples in situ on the microscope stage as lowering the temperature slows down biological processes.

Developing proximity biotinylation assays in plants to expand the interactomics toolbox

Developing proximity biotinylation assays in plants to expand the interactomics toolbox.

Proximity biotinylation uses a promiscuous biotin ligase, which causes biotinylation of proteins in the vicinity of the bait. These biotinylated proteins can be identified using mass spectrometry without the need to maintain the protein-protein interactions during the purification. This tool is therefore especially suited for interactions between cytosolic and transmembrane proteins. We are designing protocols to adequately perform proximity biotinylation in plants.

Visualizing protein-protein interactions in plants

Visualizing protein-protein interactions in plants

To gain insight into protein-protein interactions that occur in planta, we expanded the interaction assay toolkit. We have developed Knocksideways in plants (KSP) as an imaging-based protein-protein interaction assays to visualize binary as well as higher-order interactions by. KSP can be compared to an intracellular Co-IP experiment. The tool uses the ability of rapamycin to alter the localization of a bait protein and its interactors via the heterodimerization of FKBP and FRB domains.