Leica lecture: Zooming in on signal transduction by FRET – How to optimize a FRET sensor… and how to use it

Dr. Kees Jalink, Netherlands Cancer Institute (NKI-AVL), Amsterdam, NL will be giving a seminar entitled
“Zooming in on signal transduction by FRET – How to optimize a FRET sensor… and how to use it”
Tuesday 10th July at 5pm
Lecture Theatre 1, Sherrington Building, with a post lecture reception at 6.15pm in the foyer outside the lecture theatre.

 Background information from Dr Jalink’s website:

It has become clear that most, if not all, signal transduction pathways can only be truely understood by knowing them in great detail, that is, by knowing exactly where and when they become activated, how they are deactivated and what the intricacies are of e.g. compartmentalization and cross-talk. Because signaling events involve molecular interactions, it is also clear that a nanometer scale applies. This means that the tools to study signals must yield data with spatial and temporal detail from living cells, preferably from cells that are as much as possible in a natural environment.

 In our laboratory, we combine cell biology with live cell imaging and biophysical tools capable of supplying the required spatiotemporal resolution. For example, Fluorescence Resonance Energy Transfer (FRET) is used to dynamically follow molecular interactions with nanometer resolution, and techniques like high-performance Fluorescence Recovery After Photobleaching (FRAP) and Fluorescence Cross Correlation Spectroscopy (FCCS) reveal protein-protein associations at a sub-millisecond scale. We build and operate the dedicated equipment for these studies, and we contribute new technological developments and new FRET sensors.

Whereas part of the techniques employed are biophysical, our research interests are very much in cell-biology, including:

  • the “channel-kinase” TRPM7, a bifunctional protein that combines a non-selective cation channel and a serine/threonine kinase. TRPM7 regulates cell adhesion and cell spreading and, in turn, it is controlled by several signaling cascades including the Gaq-PLC route. Our working hypothesis is that TRPM7 acts as a mechanosensor that controls the formation of adhesive structures known as podosomes/invadopodia.
  • its sibling TRPM6, which serves a role in gut and kidney as gate-watcher of organismal Mg2+ homeostasis. Regulation of TRPM6 is largely unexploited.
  • the spatiotemporal control of phosphoinositides such as PIP2 and their role as messenger molecules.
  • and several collaborative projects with groups both within and outside the NKI.

 

The lecture is free, but if you wish to attend can you let Kate Goodheart (kategf@liverpool.ac.uk) know for catering purposes.

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