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Full Info Institutions/PIs

Herbst, Ruth
Herbst, Ruth

Department: Institute of Specific Prophylaxis and Tropical Medicine
Head: Herbst, Ruth, Assoc. Prof. Priv.-Doz. Dr.

Research Area

Synapse Formation, Neuromuscular Diseases, Receptor Trafficking

Description

Synapses are essential relay stations that confer information between cells. Synapses form between neurons or as in the case of the neuromuscular synapse (NMS) between a motor neuron and a muscle fiber. The NMS regulates every movement within our bodies including breathing and therefore is critical for survival. Our research focuses on the complex molecular intra- and intercellular interactions initiating NMS formation. In particular, we aim at identifying the signal transduction events and protein interactions responsible for NMS development. Our long-term goal is to understand the temporal and spatial mechanisms that lead to the formation of a mature and functional NMS.  

Techniques

Molecular biology, biochemistry, cell culture, immunohistochemistry, microscopy, transgenic animal studies, proteomics

Selected Publications

Gemza A, Barresi C, Proemer J, Hatami J, Lazaridis M, Herbst R (2022) Internalization of Muscle-Specific Kinase Is Increased by Agrin and Independent of Kinase-Activity, Lrp4 and Dynamin. Front Mol Neurosci, doi: 10.3389/fnmol.2022.780659.

Camurdanoglu BZ, Hrovat C, Dürnberger G, Madalinski M, Mechtler K, Herbst R (2016) MuSK kinase activity is modulated by a serine phosphorylation site in the kinase loop. Sci Rep, 6: 33583.

Duernberger G, Camurdanoglu BZ, Tomschik M, Schutzbier M, Roitinger E, Hudecz O, Mechtler K, Herbst R (2014), Global analysis of muscle-specific kinase signaling by quantitative phosphoproteomics. Mol Cell Proteomics, pii: mcp.M113.036087. 

Hanada T, Weitzer S, Mair B, Bernreuther C, Wainger BJ, Ichida J, Hanada R, Orthofer M, Cronin SJ, Komnenovi V, Minis A, Sato F, Mimata H, Yoshimura A, Tamir I, Rainer J, Kofler R, Yaron A, Eggan KC, Woolf CJ, Glatzel M, Herbst R, Martinez J, Penninger JM (2013), The RNA kinase CLP1 links tRNA metabolism to progressive motor neuron loss. Nature, 495 (7442), 474-80.