Brenda Schulman
Research Department Molecular Machines and Signaling (MoMaS)
Structural Biology, Ubiquitin Proteasome System, Ubiquitin-like Protein
An important form of regulation is the modification of proteins and membranes by linking them to the small protein ubiquitin or structurally related ubiquitin-like proteins (UBLs). Ubiquitin and UBLs control timing, subcellular location, composition, conformation and activity of thousands of different proteins and macromolecules. In addition, defects in ubiquitin and UBL pathways are associated with numerous diseases such as cancer, neurodegenerative disorders and viral infections. Brenda Schulman's Department “Molecular Machines and Signaling” has shown that hundreds of microscopic, dynamic, multiprotein molecular machines are transiently transformed into different conformations by specialized regulatory factors to control ubiquitin and UBLs in order to regulate virtually all aspects of cell biology.
A widespread mechanism regulating the functions of eukaryotic proteins involves post-translational modification by the small protein ubiquitin (UB) or structurally related ubiquitin-like proteins (UBLs).
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Department News
New Publication in
Nature Chemical Biology: Discovery of a charged molecular glue degrader that enters the cell uncharged and becomes activated inside, engaging the CTLH E3 ligase through its YPEL5 subunit. These findings unlock E3 ligases with charged pockets for targeted protein degradation. Great collaboration with the Gray (Stanford) and Ebert (Dana-Farber/Harvard) labs. Congratulations to all the authors!
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New Publication in Nature: This collaboration with Bartel Lab (Whitehead Institute) discovered a new principle for how RNA molecules can specify protein degradation. The ZSWIM8 E3 ligase uses a 2-RNA-factor authentication — requiring both a microRNA and a matching trigger RNA — to selectively recognize AGO complexes for degradation. Congratulations to all authors, especially to co-first authors Jakob and Elena. Special thanks to Katherine McJunkin for her
News and Views and to Base by Base for their
PaperCast. ->
Press Release
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Congratulations to Kerstin on her Boehringer Ingelheim Fonds (BIF) PhD Fellowship! Well deserved!
New Publication in Cell: Structures along formation of Proteasome Storage Granules inside yeast cells by cryo ET show assembly and functional impact of a membraneless organelle. Suprise! Paracrystalline array of 26S proteasomes! ->
Press ReleaseA great collaboration from Baumeister and Schulman labs with Cordula Enenkel/Oliver Ernst from U. Toronto. Congratulations to all authors!
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