Christoph Ballestrem, PhD
For migration over external surfaces cells need to form adhesions with the extracellular matrix and to modulate these adhesions in a spatially- and temporally-coordinated manner. Cell adhesion occurs in specialized sites, known as focal adhesions (FA), where transmembrane adhesion receptors (e.g. integrins) link the extracellular environment to the actin skeleton. The intracellular connection between integrins and microfilaments is regulated by a vast number of adaptor and signaling molecules, interconnected via a huge number of possible molecular interactions. It is apparent that these interactions do not all take place simultaneously and that they are tightly regulated. Our aim is to study molecular interactions in live cells to get a better understanding of how and through which pathways adhesion events in cells are regulated. To monitor such events we use FRET and FRAP analysis.
Recent key publications
Carisey,A., Tsang,R., Greiner, A.M., Nijenhuis, N., Heath, N., Nazgiewicz, A., Kemkemer, R., Derby, B., Spatz, J. and Ballestrem, C. (2013). Vinculin Regulates the Recruitment and Release of Core Focal Adhesion Proteins in a Force-Dependent Manner. Curr Biol 23, 271-81. PubMed
Morgan, M.R., Hamidi, H., Bass, M.D., Warwood, S., Ballestrem C. and Humphries, M.J. (2013). Syndecan-4 phosphorylation is a control point for integrin recycling. Dev Cell. 24, 472-85. PubMed
Stroud, M.J., Kammerer, R.A. and Ballestrem, C. (2011). Characterisation of GAS2-like 3, a new microtubule and actin-binding protein related to the spectraplakins. J Biol Chem doi: 10.1074/jbc.M111.242263.