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Detail

Ruth Herbst
Ruth Herbst

Center for Brain Research, Center for Pathophysiology, Infectiology and Immunology (Institute of Immunology)
Position: Associate Professor

T +43 1 40160 34260
ruth.herbst@meduniwien.ac.at

Further Information

Keywords

Endocytosis; Muscles; Neuromuscular Junction; Phosphoprotein Phosphatases; Protein Trafficking; Proteomics; Receptor Tyrosine Kinases; Signal Transduction

Research group(s)

  • Synapse Formation

Research interests

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.

Selected publications

  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.