The phosphatases PP1 and PP2A play key roles in the regulation of essential biological processes such as heartbeat, learning, and cell division. Dysregulation of these enzymes contributes to the development and progression of many diseases, such as cancer and heart failure. A research team headed by Prof. Maja Köhn from the Clusters of Excellence for biological signalling studies BIOSS and CIBSS at the University of Freiburg, together with collaborators from the European Molecular Biology Laboratory (EMBL) Heidelberg and the Technical University Munich (TUM), has developed a new mass spectrometry-based method that sheds light on the complex biological mechanisms controlling phosphatase activity. This method, which has now been published in the journal Nature Communications, will also be broadly applicable to investigate the regulation of other types of enzymes.

Phosphatases and Kinases: an uneven balance

Through a process called dephosphorylation, phosphatases remove phosphate groups from proteins. Through the opposite process of phosphorylation, another type of enzymes, so-called kinases, attach phosphate groups. Phosphate groups act as molecular switches for the control of cellular signalling processes. Intriguingly, nature has developed completely different solutions to the same problem of substrate recognition on the kinase and phosphatase.

The phosphatases PP1 and PP2A play key roles in the regulation of essential biological processes such as heartbeat, learning, and cell division. Dysregulation of these enzymes contributes to the development and progression of many diseases, such as cancer and heart failure. A research team headed by Prof. Maja Köhn from the Clusters of Excellence for biological signalling studies BIOSS and CIBSS at the University of Freiburg, together with collaborators from the European Molecular Biology Laboratory (EMBL) Heidelberg and the Technical University Munich (TUM), has developed a new mass spectrometry-based method that sheds light on the complex biological mechanisms controlling phosphatase activity. This method, which has now been published in the journal Nature Communications, will also be broadly applicable to investigate the regulation of other types of enzymes.

The phosphatases PP1 and PP2A play key roles in the regulation of essential biological processes such as heartbeat, learning, and cell division. Dysregulation of these enzymes contributes to the development and progression of many diseases, such as cancer and heart failure. A research team headed by Prof. Maja Köhn from the Clusters of Excellence for biological signalling studies BIOSS and CIBSS at the University of Freiburg, together with collaborators from the European Molecular Biology Laboratory (EMBL) Heidelberg and the Technical University Munich (TUM), has developed a new mass spectrometry-based method that sheds light on the complex biological mechanisms controlling phosphatase activity. This method, which has now been published in the journal Nature Communications, will also be broadly applicable to investigate the regulation of other types of enzymes.

The phosphatases PP1 and PP2A play key roles in the regulation of essential biological processes such as heartbeat, learning, and cell division. Dysregulation of these enzymes contributes to the development and progression of many diseases, such as cancer and heart failure. A research team headed by Prof. Maja Köhn from the Clusters of Excellence for biological signalling studies BIOSS and CIBSS at the University of Freiburg, together with collaborators from the European Molecular Biology Laboratory (EMBL) Heidelberg and the Technical University Munich (TUM), has developed a new mass spectrometry-based method that sheds light on the complex biological mechanisms controlling phosphatase activity. This method, which has now been published in the journal Nature Communications, will also be broadly applicable to investigate the regulation of other types of enzymes.