Open AccessSerine phosphorylation of the cotton cytosolic pyruvate kinase GhPK6 decreases its stability and activity
Author(s) -
Zhang Bing,
Liu JinYuan
Publication year - 2017
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12179
Subject(s) - phosphorylation , serine , pyruvate kinase , pkm2 , glycolysis , biochemistry , kinase , cytosol , pyruvate carboxylase , chemistry , protein kinase a , enzyme , protein phosphorylation , microbiology and biotechnology , biology
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.