ArticleFEBS open bio2017
Serine phosphorylation of the cotton cytosolic pyruvate kinase GhPK6 decreases its stability and activity.
Article in FEBS open bio, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Research Advances in Plant Pyruvate Kinase.International journal of molecular sciences · 2026Review
- Regulation of plant glycolysis and the tricarboxylic acid cycle by posttranslational modifications.The Plant journal : for cell and molecular biology · 2025Review
- Sucrose nonfermenting-1-related protein kinase 1 regulates sheath-to-panicle transport of nonstructural carbohydrates during rice grain filling.Plant physiology · 2022Article
- Proteome-wide identification and functional analysis of ubiquitinated proteins in peach leaves.Scientific reports · 2020Article
- Altered sucrose metabolism and plant growth in transgenic Populus tomentosa with altered sucrose synthase PtSS3.Transgenic research · 2020Article
- Copper-Induced Activation of MAPKs, CDPKs and CaMKs Triggers Activation of Hexokinase and Inhibition of Pyruvate Kinase Leading to Increased Synthesis of ASC, GSH and NADPH inFrontiers in plant science · 2020Article
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Authors and funding
2 authors.
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Abstract
Pyruvate kinase (PK, EC 2.7.1.40) is an important glycolytic enzyme involved in multiple physiological and developmental processes. In this study, we demonstrated that cotton cytosolic pyruvate kinase 6 (GhPK6) was phosphorylated at serines 215 and 402. Phosphorylation of GhPK6 at serine 215 inhibited its enzyme activity, whereas phosphorylation at both serine sites could promote its degradation. The phosphorylation-mediated ubiquitination of GhPK6 was gradually attenuated during the cotton fiber elongation process, which sufficiently explained the increase in the protein/mRNA ratios. These results collectively provided experimental evidence that cotton fiber elongation might be regulated at the post-translational level.
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