Serine phosphorylation of the cotton cytosolic pyruvate kinase GhPK6 decreases its stability and activity

Zhang, Bing; Liu, Jinyuan

doi:10.1002/2211-5463.12179

Cited by 16 publications

(4 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Ubiquitin-dependent degradation of glycolytic enzymes has been previously shown to exert strong modulatory effects on plantand animal physiology. Zhang et al reported that phosphorylation-activated ubiquitination of cytosolic pyruvate kinase 6 in cotton might be associated with accelerated fiber elongation 40 . In another study, Almeida and colleagues showed that APC/C-induced degradation of 6-phosphofructokinase significantly suppressed glycolysis, and thus proliferation, in tumor cells 41 .…”

Section: Discussionmentioning

confidence: 99%

Proteome-wide identification and functional analysis of ubiquitinated proteins in peach leaves

Song

Shi

Zou

et al. 2020

Sci Rep

View full text Add to dashboard Cite

Ubiquitination is a critical post-translational modification machinery that governs a wide range of cellular functions by regulating protein homeostasis. Identification of ubiquitinated proteins and lysine residues can help researchers better understand the physiological roles of ubiquitin modification in different biological systems. In this study, we report the first comprehensive analysis of the peach ubiquitome by liquid chromatography-tandem mass spectrometry-based diglycine remnant affinity proteomics. Our systematic profiling revealed a total of 544 ubiquitination sites on a total of 352 protein substrates. Protein annotation and functional analysis suggested that ubiquitination is involved in modulating a variety of essential cellular and physiological processes in peach, including but not limited to carbon metabolism, histone assembly, translation and vesicular trafficking. Our results could facilitate future studies on how ubiquitination regulates the agricultural traits of different peach cultivars and other crop species.Peach is a highly popular and well-recognized fruit first cultivated in China during ancient times. It is considered an excellent source of vitamin C, niacin, potassium and dietary fiber. As a result, the recent global trend of healthy eating has greatly stimulated the demand for peach and the related food products. As of 2014, the combined area of peach orchards in China is estimated at around 7,260 square kilometers, with a total production of 12.4 million tons 1 . The long history of peach cultivation has resulted in hundreds of distinct cultivars. Peach growers have spent decades in a continuous quest to enhance the quality of different peach cultivars through crossbreeding. Recently, biotechnology-facilitated engineering has shown enormous promise in rapidly generating new peach varieties with desirable agricultural traits. Still, further accomplishments would depend on improved understanding of the diverse molecular pathways in peach and their connections to its physiology.Ubiquitination is one of the most critical post-translational modification mechanisms with a wide range of cellular functions that center on the control of protein load 2,3 . Ubiquitin is a small but abundantly present protein consisting of 76 amino acids with a C-terminal diglycine tail. The ubiquitination pathway is essentially an enzymatic cascade involving the cooperative action of three enzymes, including the E1, E2 and E3 ligases 2,4 . During this process, the C-terminal carboxyl group of ubiquitin is first adenylated by E1 in the presence of ATP and then forms a thioester linkage with the catalytic cysteine residue of the ligase 5 . The E1 then binds a second ubiquitin with its adenylation domain and recruits its cognate E2.This triggers a transthioesterification reaction where the E1-conjugated ubiquitin unit is transferred to the catalytic cysteine of the E2 6 . Finally, an E3 is involved in the transfer of ubiquitin from E2 to the ε-amino group of one or more lysine residues in the protein substrate 7...

show abstract

Section: Discussionmentioning

confidence: 99%

Proteome-wide identification and functional analysis of ubiquitinated proteins in peach leaves

Song

Shi

Zou

et al. 2020

Sci Rep

View full text Add to dashboard Cite

show abstract

“…In this work, we initially showed that copper induces the increase in HK activity through MAPKs activation whereas it inhibits PK through CDPKs and MAPKs activation indicating that phosphorylation of HK and PK enzymes regulate these activities. In this sense, it has been shown that PK activity is inhibited by phosphorylation of ser215 in soybean and cotton cells and the additional phosphorylation in ser402 enhances its degradation in the proteasome ( Tang et al., 2003 ; Zhang and Liu, 2017 ). In addition, it has been shown that HK1 and HK2 are activated by c-Src tyrosine kinase that phosphorylates tyr73, which favors proliferation, migration and invasion of human tumoral cells ( Zhang et al., 2017 ).…”

Section: Discussionmentioning

confidence: 99%

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 in Ulva compressa

2020

View full text Add to dashboard Cite

In order to analyze whether copper induces activation of CaMK, CDPK and/or MAPK signaling pathways leading to carbon flux reprogramming and to the synthesis of ascorbate (ASC), glutathione (GSH) and NADPH in order to buffer copper-induced oxidative stress, U. compressa was initially cultivated with 10 µM copper for 0 to 10 days. The activities of hexokinase (HK), pyruvate kinase (PK), L-galactone 1,4 lactone dehydrogenase (L-GLDH) and glucose 6-P dehydrogenase (G6PDH) were analyzed. HK activity was increased whereas PK was inhibited, and L-GLDH and G6PDH activities were increased indicating a copper-induced modulation of glycolysis leading to carbon flux reprogramming. Then, the alga was cultivated with an inhibitor of CaMs and CaMKs, CDPKs and MAPKs, and with 10 µM of copper for 5 days and the activities of HK, PK, L-GLDH, G6PDH and glutathione synthase (GS), the levels of ASC/DHA, GSG/GSSG and NADPH/NADP, the levels of superoxide anions (SA) and hydrogen peroxide (HP) and the integrity of plasma membrane were determined. The activation of HK was dependent on MAPKs, the inhibition of PK on CDPKs/MAPKs, the activation of L-GLDH on MAPKs, the activation GS on CDPKs/MAPKs, and the activation of G6PDH on MAPKs. Increases in the level of ASC/DHA were dependent on activation of CaMKs/CDPKs/MAPKs, those of GSG/GSSG on MAPKs and those NADPH/NADP on CaMKs/CDPKs/MAPKs. The accumulation of superoxide anions and hydrogen peroxide and the integrity of plasma membrane were dependent on CaMKs/CDPKs/MAPKs. Thus, copper induced the activation of MAPKs, CDPKs and CaMKs leading to the modulation of glycolysis and carbon flux reprogramming which trigger an increase in ASC, GSH and NADPH syntheses and the activation of antioxidant enzymes in order to buffer copper-induced oxidative stress in U. compressa.

show abstract

“…Phosphorylation increases the stability of PK under acidic condition (Schwägele et al ., ). Phosphorylation of pyruvate kinase at serine 215 inhibits its enzyme activity, so it can be hypothesised that the stability of PK was increasing and the activities was inhibited after phosphorylation (Zhang & Liu, ). The phosphorylation level of PK was higher in the S group, which corresponded to the determined glycolytic rate.…”

Section: Discussionmentioning

confidence: 99%

The effect of sarcoplasmic protein phosphorylation on glycolysis in postmortem ovine muscle

Chen

et al. 2018

Int J of Food Sci Tech

View full text Add to dashboard Cite

Protein phosphorylation is a key modulator in glycolysis metabolism and regulates the activity of glycometabolic enzymes. The phosphorylation levels of sarcoplasmic proteins were investigated in relationship to the glycolysis rate in postmortem ovine muscle in the present study. The global phosphorylation levels of sarcoplasmic proteins increased early postmortem and then decreased afterwards in postmortem ovine muscle. Protein bands of different phosphorylation levels were identified as glycometabolism‐related enzymes. The phosphorylation levels of Glycogen phosphorylase and Pyruvate kinase maybe one possible reason for the different glycolytic rates at 0.5 h postmortem. The glycolytic rate attributes were negatively correlated with four bands which were probably phosphofructokinase, enolase and adenylate kinase isoenzyme. In summary, the phosphorylation of sarcoplasmic proteins is related to muscle pH decline early postmortem, influencing the meat rigour mortis and quality development.

show abstract

Serine phosphorylation of the cotton cytosolic pyruvate kinase GhPK6 decreases its stability and activity

Cited by 16 publications

References 32 publications

Proteome-wide identification and functional analysis of ubiquitinated proteins in peach leaves

Proteome-wide identification and functional analysis of ubiquitinated proteins in peach leaves

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 in Ulva compressa

The effect of sarcoplasmic protein phosphorylation on glycolysis in postmortem ovine muscle

Contact Info

Product

Resources

About