The abstract is read at the publisher; the summary is JClub's.
SPINDLY (SPY)-catalyzed O-fucosylation antagonizes BIN2-mediated phosphorylation of PCK1 in Arabidopsis thaliana, preventing phosphorylation at Ser-62/Thr-66 and regulating gluconeogenesis.
- Why it matters: Overlapping sugar-dependent glycosylation and BR-linked phosphorylation are known to target similar proteins, but their functional interplay in metabolism and growth was unclear.
- What they did: The study tested whether SPY competes with BIN2 on PCK1 by mapping an O-fucosylation peptide containing Ser-62 and Thr-66, assessing mutual exclusion of modifications, and measuring PCK1 phosphorylation/activity and hypocotyl elongation in spy mutants with BR or BIN2 inhibitor treatments.
- The result: In vivo, PCK1 O-fucosylation and phosphorylation exclude each other and oppositely affect PCK1 activity; spy mutants show increased PCK1 phosphorylation, reduced PCK activity, and impaired hypocotyl elongation, which BR or BIN2 inhibitor treatments suppress.
The findingWhy it mattersWhat they didThe result
AI summary of the abstract · may contain errors · not medical advice · read the paper.