
Institute of Specific Prophylaxis and Tropical Medicine (Center for Pathophysiology, Infectiology and Immunology)
Position: Associate Professor
Location: Kinderspitalgasse 15
Phone: +43 1 40160-33276
E-Mail: ruth.herbst@meduniwien.ac.at
Research Area
Muscle, Skeletal, Neuromuscular Disorders, Neuromuscular Junction
Research Interests
Endocytosis, Signal Transduction, Synapses
Principle Investigator(s)
Interest Group(s)
Grant(s)
Abstract
Synapses are essential relay stations that confer information between cells. Synapses form between neurons or as in the case of the neuromuscular junction (NMJ) between a motoneuron and a muscle fiber. The NMJ 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 NMJ formation. In particular, we aim at identifying the signal transduction events and protein interactions responsible for NMJ development. Our long-term goal is to understand the temporal and spatial mechanisms that lead to the formation of a mature and functional NMJs.
Selected publications
- Herbst R, Huijbers M, Oury J, Burden S (2024) Building, Breaking, and Repairing Neuromuscular Synapses Cold Spring Harb Perspect Med., 16 (5): a041490
- Kim J, Caine C, Awano T, Herbst R, Monani U (2017) Motor neuronal repletion of the NMJ organizer, Agrin, modulates the severity of the spinal muscular atrophy disease phenotype in model mice Hum Mol Genet, Epub ahead of print
| doi:10.1093/hmg/ddx124 | - 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
| Weblink | - 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, 13 (8): 1993-2003
| Weblink | - Herbst, R. and Burden, S.J. (2000) The juxtamembrane region of MuSK has a critical role in agrin-mediated signaling. EMBO J., 19: 67-77