Research Topics / Cytoplasmic signalling
PhD Training

Within the MCBO training program we offer several lectures on basic concepts of signal transduction, regulation of protein kinases, and hands-on courses on proteomics, animal experimentation, production of recombinant kinases, and other topics.

Protein phosphorylation is an important means of reversible posttranslational protein modification that affects 30-50% of all proteins and is involved in every aspect of physiological or pathophysiological cell function. In eukaryotes, proteins are mainly phosphorylated on serine, threonine or tyrosine residues with a relative frequency of 100:10:1. Because protein phosphorylation changes the electrostatic surface properties of a protein it affects its structure and ability to interact with other molecules, which can result in altered protein function, subcellular localization, stability, etc. Protein kinases recognize their substrates via specific protein interaction motifs and phosphorylate specific residues only within certain amino acid residue contexts, which are generalized as phosphorylation consensus motifs. In addition, kinases, their upstream regulators as well as their substrates are often compartmentalized to achieve high substrate specificity and to avoid generation of noise and signaling circuit shortcuts. Because protein kinases belong to the class of ‘druggable’ proteins they are important subjects for study in biomedical research.
Protein kinases modulate a wide variety of biological processes, especially those that
carry signals from the cell membrane to intracellular targets and coordinate complex
biological functions. Protein kinases constitute one of the largest human gene families
and are key regulators of cell function. More then 520 human protein kinases control
protein activity by catalyzing the addition of a negatively charged phosphate group to
other proteins.

The Kinome: This phylogenetic tree depicts the relationships
between members of the complete superfamily of human
protein kinases. The diagram illustrates the similarity between
the protein sequences of these catalytic domains. Each kinase
is at the tip of a branch, and the similarity between various
kinases is inversely related to the distance between their
positions on the tree diagram. The seven major groups are
labeled and colored distinctly.
Protein kinase research in Innsbruck

Protein kinases research plays an important role for several research groups at Innsbruck Medical University. The main focus is on PKC function in T-cells, regulation of MAPK signaling by adaptor proteins, and regulation and specificity of CDKs. The involved groups use genetic as well as biochemical methods to identify the essential functions of the involved proteins and to define kinase substrates to arrive at a mechanistic understanding of how these functions control immunological responses as well as cellular differentiation and proliferation. Substrates are identified by several means, including many phosphoproteomic approaches.


Recombinant protein expression in bacteria and insect cells; phosphoproteomics, transgenic and knockout mouse models.