Detail

Keywords

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

Research group(s)

• Transport and Signal Transduction of Surface Receptors
  Head: Ruth Herbst
  Research Area: We are interested in how receptor tyrosine kinases induce intracellular signaling cascades thereby regulating crucial cellular process including cell proliferation, differentiation and survival. Further, we are interested in trafficking processes such as endocytosis and recycling of surface proteins. We study process in the muscle and in immune cells
  Members:
  Jakob Proemer
  Ruth Herbst

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.

For more information visit https://www.meduniwien.ac.at/hp/tropenmedizin/forschung/transport-signaluebertragung-von-oberflaechenrezptoren/

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. Gemza, A. et al. (2022) ‘Internalization of Muscle-Specific Kinase Is Increased by Agrin and Independent of Kinase-Activity, Lrp4 and Dynamin’, Frontiers in Molecular Neuroscience, 15. Available at: http://dx.doi.org/10.3389/fnmol.2022.780659.
2. Camurdanoglu, B.Z. et al., 2016. MuSK Kinase Activity is Modulated By A Serine Phosphorylation Site in The Kinase Loop. Scientific Reports, 6(1). Available at: http://dx.doi.org/10.1038/srep33583.
3. Dürnberger, 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.
4. 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.
5. 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.