Detail

Keywords

Anatomy; Cell Culture Techniques; Histology, Comparative; Microscopy; Molecular Biology

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 processes in the muscle and in immune cells.
  Members:
  Ruth Herbst
  Jakob Prömer

Research interests

The neuromuscular junction connects nervous system and muscle tissue. Muscle specific kinase (MuSK) is a receptor tyrosine kinase that is crucial for its formation. I aim to characterize a specific serine residue in MuSK that relates to its activation. I will identify the kinase that phosphorylates this serine, and analyse the kinase domains of wildtype- and phosphomimetic mutant MuSK in a structure-function approach. A transgenic mouse model will provide understanding of the effect of serine phosphorylation in vivo. These data will provide insight in the mechanism of MuSK activation and potential rescue mechanisms for the development of the neuromuscular junction.

Techniques, methods & infrastructure

Mammalian and insect cell culture, Western Blot, Molecular Cloning, Protein purification techniques, Histology and Immunocytochemistry, Fluorescence- and confocal laser scanning microscopy,

Selected publications

1. Prömer, J. J. et al. (2026) “An S752D activation loop mutation dynamically primes Muscle-Specific Kinase for activation,” Biochemical Journal. Edited by , 483(7), pp. 1221–1235. Available at: https://doi.org/10.1042/bcj20260159.
2. Barresi, C. et al. (2026) “Crk/Crk-L-mediated Rapgef1 recruitment couples MuSK signaling to AChR anchoring at the neuromuscular junction,” Cell Chemical Biology [Preprint]. Edited by . Available at: https://doi.org/10.1016/j.chembiol.2026.08.014.
3. Prömer, J.J. et al. (2025) “MuSK is a substrate for CaMK2β but this interaction is dispensable for MuSK activation in vivo,” Scientific Reports. Edited by , 15(1). Available at: https://doi.org/10.1038/s41598-025-95053-3.
4. Prömer, J., Barresi, C. and Herbst, R. (2023) “From phosphorylation to phenotype – Recent key findings on kinase regulation, downstream signaling and disease surrounding the receptor tyrosine kinase MuSK,” Cellular Signalling. Edited by , 104, p. 110584. Available at: https://doi.org/10.1016/j.cellsig.2022.110584.
5. Prömer, J., Sombke, A. and Schwaha, T. (2021) “A comparative analysis of the nervous system of cheilostome bryozoans,” BMC Zoology. Edited by , 6(1). Available at: https://doi.org/10.1186/s40850-021-00084-8.