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March 2022
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Cover Image
Cover Image
Parkin is an E3 ligase that binds phosphorylated ubiquitin, and is itself phosphorylated, to trigger substrate ubiquitinatation. In this issue Dunkerley et al (p 751–766) use chimeric substrates comprising the C-terminal GTPase domain of Miro1 fused to ubiquitin to uncouple these two phosphorylation events. The cover image shows a series of fluorescence gel-based assays that simultaneously monitor the ubiquitination of a substrate protein (red) and formation of ubiquitin chains (green) by parkin. The work shows that recruitment of phosphorylated ubiquitin tethered to a mitochondrial protein, not phosphorylation of parkin, is essential to recruit and ubiquitinate a target substrate.
ISSN 0264-6021
EISSN 1470-8728
In this Issue
Review Articles
Immunothrombosis and the molecular control of tissue factor by pyroptosis: prospects for new anticoagulants
Biochem J (2022) 479 (6): 731–750.
Research Articles
Overexpression of phospholipid: diacylglycerol acyltransferase in Brassica napus results in changes in lipid metabolism and oil accumulation
Stepan Fenyk; Helen K. Woodfield; Trevor B. Romsdahl; Emma J. Wallington; Ruth E. Bates; David A. Fell; Kent D. Chapman; Tony Fawcett; John L. Harwood
Biochem J (2022) 479 (6): 805–823.