Dataset Information

Dynamic responses of barley root quantitative succinyl-proteome to short-term phosphate starvation and recovery

ABSTRACT: Improving phosphate (Pi) acquisition and utilization efficiency is a crucial challenge for the sustainability of agriculture worldwide. The understanding of plant how to response and cope with Pi-limitation, and its underlying molecular mechanisms is key to discovering strategies of efficient Pi acquisition and utilization. Barley (Hordeum vulgare L.) is one of the major cereal crops, has distinct advantage for studying mechanisms of tolerance of phosphorus deficiency due to low Pi demand. Recent studied reveal that post-translational modification (PTM) by phosphorylation, ubiquitination, and glycosylation are play important roles in cellular regulation the plant phosphate starvation response (PSR). Lysine succinylation occurs frequently in the proteins associated with metabolic pathways, which may participate in the regulation of the plant PSR process. However, succinylation precisely modulates the metabolic pathways of proteins in response to PSR in barley remain largely unknown.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Hordeum Vulgare (barley)

TISSUE(S): Root

SUBMITTER: Juncheng Wang

LAB HEAD: Wang juncheng

PROVIDER: PXD022077 | Pride | 2021-07-13

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	F9259LPST_D1CK6H_01_Slot2-40_1_698.d.zip	Other
	F9259LPST_D1CK6H_02_Slot2-40_1_699.d.zip	Other
	F9259LPST_D1CK6H_03_Slot2-40_1_700.d.zip	Other
	F9259LPST_H1E_48H_01_Slot2-44_1_716.d.zip	Other
	F9259LPST_H1E_48H_02_Slot2-44_1_717.d.zip	Other

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Project description:Phosphorylation is well-known in regulating various biological processes. However, comprehensively phosphoproteomic profiling in the termination of liver regeneration (LR) is still missing. Here, we used TMT labeling coupled with phosphopeptides enrichment and 2D LC-MS/MS analysis to establish a global phosphoproteomic map in mice liver at day 5 after partial hepatectomy. Altogether, 619 phosphorylation sites in 437 proteins were significantly up-regulated and 503 phosphorylation sites in 358 proteins were down-regulated. The differentially phosphorylated proteins were further classified according to their biological process, cellular components, molecular function and subcellular localization. KEGG pathway analysis showed that they mainly participate in metabolic pathways, DNA replication, tight junction and focal adhesion. Motif analysis of the identified phosphorylation sites has revealed a diverse array of consensus sequences, suggesting multiple kinase families such as MAPK, PKA/PKC, CaMK-II, CKII and CDK, may be involved in the termination of LR. Finally, several differentially phosphorylated proteins were validated by Co-immunoprecipitation and Western blot. Taken together, our data unravels the first comprehensive phosphoproteomic map in the termination of liver regeneration in mice, which greatly expands our knowledge in the complicate regulation of this process and provides new directions on the treatment of liver cancer using liver resection and donor liver transplantation. Biological significance: The novelty of this study is that we have established for the first time a global phosphoproteomic map in mice liver at day 5 after partial hepatectomy, which represents the termination of liver regeneration. Altogether, 9,775 phosphorylation sites in 3,458 proteins were identified, among which 7,738 phosphorylation site in 2,971 proteins were quantified. KEGG pathway analysis demonstrates markedly metabolic reprograming in termination of LR, which is further validated by selected validation of several differentially phosphorylated metabolic enzymes such as PDHA, ACACA and FASN. The consistent high phosphorylation of PDHA in the first 4 days and its rapidly decreased phosphorylation at day 5 after PH might be a key signal in controlling the switch between glycolysis and oxidative

Dataset Information

Dynamic responses of barley root quantitative succinyl-proteome to short-term phosphate starvation and recovery

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