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

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

Andreas Janshoff

B4: “In vitro reconstitution of inhibitory GABAergic postsynapses”

Claudia Steinem

A6: “Mitochondria function and turnover in synapses”

Peter Rehling