Immune signalling pathways in cancer & autoimmunity

Dr. rer. nat. Vijay K. Ulaganathan

Understanding how the adaptive immune system works in humans is essential for understanding conditions such as cancer malignancies and autoimmune toxicities. The focus of this group is immune signalling mechanisms in T cells, the essential regulators of adaptive immune responses. On the one hand, immune evasion in tumour tissues due to insufficient T-cell aggressiveness is a major driver of disease progression in cancer patients, while on the other hand, overshooting T-cell reactions lie at the basis of autoimmune toxicities. Earlier work from my group have shown that tumour evading traits of the T cells are dictated by proximal signals triggered by the phosphotyrosine signalling motifs that recruit STAT3 to inner membranes (Ulaganathan et al, Nature 2015; Ulaganathan et al Mol Cell Oncol. 2016; Kogan et al, JCI 2018, Ulaganathan VK Scientific Reports 2020). In general, membrane-bound signals are transmitted through the cytoplasm to the nucleus in T cells in the form of phosphate transfer reactions that are dictated by membrane-bound kinases and phosphatases. My research group aims to understand and manipulate specific phosphotyrosine signalling pathway mechanisms in the tumour-antigen reactive T cells and generate new mechanistic knowledge linking T cell-mediated immune evasion and immune attack.


  • Martina Vasileva (Master Thesis)
  • Jumana Kamel (Lab rotation – candidature considered)



Dr. rer. nat. Vijay K. Ulaganathan


Publications during the year 2015–2020

  • *Ulaganathan VK. TraPS-VarI: Identifying genotype-specific immunoreceptor tyrosine based sequence motifs. Scientific Reports. 10, Article number: 8453 (2020). [Impact Factor: 4.011], doi:
  • Kogan D, Grabner A, Yanucil C, Faul C, *Ulaganathan VK. STAT3-enhancing germline mutations contribute to tumor-extrinsic immune evasion. J Clin Invest. (2018) Feb 13. [Impact Factor: 12.282], doi:
  • *Ulaganathan VK, Sperl B, Rapp UR, *Ullrich A. Germline variant FGFR4 p.G388R exposes a membrane-proximal STAT3 binding site. Nature. 2015 Dec 24; 528 (7583):570-4. [Impact Factor: 43.070], doi:

* corresponding author

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