Chaperone
- An evolutionarily distinct chaperone promotes 20S proteasome α-ring assembly in plants
Highlighted Article: PBAC5 is an evolutionarily distinct chaperone that forms a tripartite complex with PBAC1 and PBAC2 to promote assembly of the 20S proteasome α-ring in Arabidopsis.
- A trap mutant reveals the physiological client spectrum of TRC40
Summary: A strategy to decipher which tail-anchored proteins do (as opposed to can or must) use the TRC pathway in intact cells generates a comprehensive list of human TRC40 clients.
- Hsp70–Hsp110 chaperones deliver ubiquitin-dependent and -independent substrates to the 26S proteasome for proteolysis in yeast
Summary: Hsp110 associates with the proteasome and ensures the efficient delivery of Hsp70 chaperone-associated proteins for proteolysis in the yeast S. cerevisiae.
- BAG3-mediated proteostasis at a glance
Summary: We discuss how the co-chaperone BAG3 maintains the proteome by balancing transcription, translation and autophagy, and how impairment or deregulation of BAG3 can cause muscle weakness, neurodegeneration and cancer.
- Distinguishing aggregate formation and aggregate clearance using cell-based assays
Highlighted Article: Disequilibrium between aggregate formation and clearance leads to accumulation of aggregated proteins. We have created a new cell-based assay that can determine how modifiers can impact on aggregate burden.
- The clathrin-binding and J-domains of GAK support the uncoating and chaperoning of clathrin by Hsc70 in the brain
Summary: Our studies on GAK- and auxilin-knockout mice show that the only essential domains of GAK and auxilin in the brain are the clathrin-binding domain and the J-domain that binds to Hsc70.