K. Hofmann

ERLIN1/2 scaffolds bridge TMUB1 and RNF170 and restrict cholesterol esterification to regulate the secretory pathway

This study identifies ERLIN1/2 scaffolds that mediate TMUB1-RNF170 interactions, regulate cholesterol esterification, and maintain ER cholesterol levels to control Golgi morphology and the secretory pathway.

The structural basis for deubiquitination by the fingerless USP-type effector TssM

This study determines the crystal structures of TssM, a USP-type deubiquitinase from B. pseudomallei and B. mallei, revealing its unique structural features and mechanism of ubiquitin recognition.

FAM104 proteins promote the nuclear localization of p97/VCP

This study identifies FAM104 proteins as novel p97 interactors that facilitate nuclear import and chromatin binding of p97, highlighting their role in cellular processes and disease.

Lysine deserts prevent adventitious ubiquitylation of ubiquitin-proteasome components

The paper identifies lysine deserts in UPS proteins and shows that introducing lysines increases ubiquitylation, with functional consequences for protein stability and function.

N4BP1 is dimerization-dependent linear ubiquitin reader regulating TNFR1 signalling through linear ubiquitin binding and Caspase-8-mediated processing

This study identifies N4BP1 as a dimerization-dependent linear ubiquitin reader that regulates TNFR1 signaling by modulating NF-κB and apoptosis pathways.

An evolutionary approach to systematic discovery of novel deubiquitinases, applied to Legionella

The paper identifies novel deubiquitinases in Legionella pneumophila by analyzing conserved features across DUB families and validating their substrate specificity.

Identification and characterization of diverse OTU deubiquitinases in bacteria

The paper identifies and characterizes OTU deubiquitinases in bacteria, showing their structural and functional similarities to human and viral OTUs.

Plant mixed lineage kinase domain-like proteins limit biotrophic pathogen growth

The paper identifies a plant MLKL protein family structurally similar to vertebrate MLKL, which provides immunity against pathogens without inducing cell death.