Skip Nav Destination
In this issue Byrne and colleagues (pp. 141–160) confirm that, as predicted, PSKH2 lacks detectable protein phosphotransferase activity, and exploit structural informatics, biochemistry and cellular proteomics to begin to characterise vertebrate PSKH2 orthologues. They show that PSKH2 is part of a cellular mitochondrial protein network, and that its expression is regulated through client-status within the HSP90/Cdc37 molecular chaperone system. The cover image shows an Alpha Fold 2 model of human PSKH2 (grey, green and brown) bound to HSP90 (cyan) and Cdc37 (magenta). The image is courtesy of Patrick Eyers.
In this Issue
Structural features of sensory two component systems: a synthetic biology perspective
Biochem J (2023) 480 (2): 127–140.
BH3 mimetics and TKI combined therapy for Chronic Myeloid Leukemia
Biochem J (2023) 480 (2): 161–176.