Endocytosis; Muscles; Neuromuscular Junction; Phosphoprotein Phosphatases; Protein Trafficking; Proteomics; Receptor Tyrosine Kinases; Signal Transduction
- Synapse Formation
My work is focused on characterizing how receptor tyrosine kinases induce intracellular signaling cascades thereby regulating crucial cellular processes including cell proliferation, differentiation and function. My long-term interests center around the receptor tyrosine kinase MuSK. As postdoctoral fellow and subsequently as independent group leader, together with my laboratory, I made important contributions to the function of MuSK and to the characterization of downstream signaling events. More recently I have also become interested in protein trafficking and the interplay between signaling and protein endocytosis. In this respect, we have identified a novel guanidine nucleotide exchange factor with potential function in T cell responses during inflammatory conditions.
Techniques, methods & infrastructure
Experimental strategies include muscle cell cultures and their manipulation (retroviral-mediated gene transduction), confocal microscopy as well as in vivo imaging and analysis of transgenic animal models. Biochemistry, molecular biology and cell biology techniques complete our approaches.
- Durnberger, G. et al., 2014. Global Analysis of Muscle-specific Kinase Signaling by Quantitative Phosphoproteomics. Molecular & Cellular Proteomics, 13(8), pp.1993-2003. Available at: http://dx.doi.org/10.1074/mcp.M113.036087.
- Luiskandl, S. et al., 2013. Endosomal trafficking of the receptor tyrosine kinase MuSK proceeds via clathrin-dependent pathways, Arf6 and actin. FEBS Journal, 280(14), pp.3281-3297. Available at: http://dx.doi.org/10.1111/febs.12309.
- Hanada, T. et al., 2013. CLP1 links tRNA metabolism to progressive motor-neuron loss. Nature, 495(7442), pp.474-480. Available at: http://dx.doi.org/10.1038/nature11923.
- Woller, B. et al., 2011. Rin-like, a novel regulator of endocytosis, acts as guanine nucleotide exchange factor for Rab5a and Rab22. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1813(6), pp.1198-1210. Available at: http://dx.doi.org/10.1016/j.bbamcr.2011.03.005.
- Nizhynska, V. et al., 2007. Phosphpinositide 3-kinase acts through the small GTPases Rac and Cdc42 during agrin-induced acetylcholine receptor clustering. Dev. Neurobiol, 67, pp.1047-1058.