SUMOylation is a post-translational protein modification akin to ubiquitination, which involves the conjugation of the ubiquitin like proteins SUMO1, SUMO2, and SUMO3. It is a key protein modification required by every eukaryotic cell, is relevant to almost every cellular process, and can have very diverse consequences, e.g. on protein solubility, stability, and interactions. We propose to employ a set of novel genetically modified mouse models for a systematic, analysis of synaptic SUMO conjugation, and of altered synaptic SUMOylation

Nils Brose

Principal Investigator
More subprojects

B6: “The role of RNA in synapse physiology and neurodegeneration”

André Fischer/Tiago Outeiro

B3: “Mapping the protein and lipid organization in the plasma membrane of neurons using rapid rupture event imaging”

Andreas Janshoff

C3: “Modelling dendritic spine fluctuations”

Florentin Wörgötter