Stress conditions can cause the relocalization of proteasomes to condensates in yeast and
mammalian cells. The interactions that facilitate the formation of proteasome condensates …

Highly homologous ubiquitin-binding shuttle proteins UBQLN1, UBQLN2, and UBQLN4
differ in both their specific protein quality control functions and their propensities to localize …

The rapid evolution of protein structure prediction tools has significantly broadened access
to protein structural data. Although predicted structure models have the potential to …

Conformational switching is pervasively driven by protein interactions, particularly for
intrinsically disordered binding partners. We developed a dually orthogonal fluorescence …

Ubiquitination is one of the most common post-translational modifications in eukaryotic cells.
Depending on the architecture of polyubiquitin chains, substrate proteins can meet different …

Highly homologous ubiquitin-binding shuttle proteins UBQLN1, UBQLN2 and UBQLN4 differ
in both their specific protein quality control functions and their propensities to localize to …

Ubiquilins are a family of cytosolic proteins that ferry ubiquitinated substrates to the
proteasome for degradation. Recent work has demonstrated that Ubiquilins can also act as …

Ubiquilins are a family of proteins critical to cellular proteostasis that are also linked to
neurodegenerative diseases such as ALS, with specific mutations in UBQLN2 causing …

In this issue of Structure, Buel et al.(2023) combined NMR data with AlphaFold2 to map out
the interaction between the AZUL domain of ubiquitin ligase E6AP and UBQLN1/2 UBA. The …

UBQLN1 functions in autophagy and proteasome-mediated protein degradation. It contains
an N-terminal ubiquitin-like domain (UBL), a C-terminal ubiquitin-associated domain (UBA) …