Markus Moser

Interest

We are interested in the mechanism of integrin signalling. Integrins shift between an inactive and active conformation. Activation is induced upon binding of the cytoplasmic protein talin to the beta integrin cytoplasmic domain. We could recently show that in addition to talin, a second integrin binding protein, named kindlin, is essential for integrin activation (integrin inside-out signalling).

Kindlins represent a family of three proteins and received their name after a human disease, named Kindler syndrome, which is caused by mutations in the kindlin-1 gene. Previous data from another group and our own observations also imply a function of kindlins in integrin signalling into the cell (integrin outside-in signalling) and in linking the integrin adhesion complex with the cytoskeleton.

My group is particularly interested in the function of kindlin-3, which is exclusively expressed in hematopoietic cells. Kindlin-3 knockout mice exhibit a number of phenotypes based on defects in certain hematopoietic cell populations. We could recently show that kindlin-3 is essential for integrin activation and aggregation of platelets.

We are currently investigating the role of kindlin-3 in other hematopoietic cells such as erythrocyts, osteoclasts and macrophages. Beside this, we are particularly interested in proteins that interact with kindlin-3 and are involved in integrin signalling. To this end, we are using the SILAC method, which allows quantitative proteomics.