Affiliation: Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, London, UK
Role: Associate Editor
Keywords: Ubiquitination, protein structure, protein structure/assembly, ubiquitin ligases, protein signalling modules/scaffolds, enzyme structure-function
Subject Areas: Molecular structure and function
Biography: Katrin Rittinger studied Chemistry at the University of Heidelberg and carried out her Ph.D. with Roger Goody at the Max-Planck Institute for Medical Research in Heidelberg. In 1996, she received an EMBO Long-Term and subsequently a Marie-Curie Fellowship to move to the MRC National Institute for Medical Research (NIMR) in London to work with Guy Dodson and Alastair Aitken on the structural basis of the interaction between 14-3-3 proteins and phosphorylated target proteins. In parallel she became interested in members of the Rho-family of GTPases and helped to elucidate the mechanism of action of GTPase-activating proteins (GAPs). In 2000 she set up her own independent group at the MRC-NIMR studying the molecular basis of signalling processes that are regulated by Rho family GTPases. More recently, she has developed an interest in the ubiquitination-dependent regulation of immune signalling processes. Her group has recently moved to the Francis Crick Institute in London.