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The glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase and hexokinase interact with cell cycle proteins in maize.

Authors :
Vargas-Cortez T
Guerrero-Molina ED
Axosco-Marin J
Vázquez-Ramos JM
Lara-Núñez A
Source :
FEBS letters [FEBS Lett] 2023 Aug; Vol. 597 (16), pp. 2072-2085. Date of Electronic Publication: 2023 Aug 06.
Publication Year :
2023

Abstract

Cyclin/cyclin-dependent kinase (CDK) heterodimers have multiple phosphorylation targets and may alter the activity of these targets. Proteins from different metabolic processes are among the phosphorylation targets, that is, enzymes of central carbon metabolism. This work explores the interaction of Cyc/CDK complex members with the glycolytic enzymes hexokinase 7 (HXK7) and glyceraldehyde-3-phosphate dehydrogenase (GAP). Both enzymes interacted steadily with CycD2;2, CycB2;1 and CDKA;1 but not with CDKB1;1. However, Cyc/CDKB1;1 complexes phosphorylated both enzymes, decreasing their activities. Treatment with a CDK-specific inhibitor (RO-3306) or with lambda phosphatase after kinase assay restored total HXK7 activity, but not GAP activity. In enzymatic assays, increasing concentrations of CDKB1;1, but not of CycD2;2, CycB2;1 or CycD2;2/CDKB1;1 complex, decreased GAP activity. Cell cycle regulators may modulate carbon channeling in glycolysis by two different mechanisms: Cyc/CDK-mediated phosphorylation of targets (e.g., HXK7; canonical mechanism) or by direct and transient interaction of the metabolic enzyme (e.g., GAP) with CDKB1;1 without a Cyc partner (alternative mechanism).<br /> (© 2023 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)

Details

Language :
English
ISSN :
1873-3468
Volume :
597
Issue :
16
Database :
MEDLINE
Journal :
FEBS letters
Publication Type :
Academic Journal
Accession number :
37489921
Full Text :
https://doi.org/10.1002/1873-3468.14704