Dataset Information

Ciona savignyi notochord LC-MS/MS based on 4D Mass Spectromete

ABSTRACT: Lumen formation and inflation are crucial for tubular organ morphogenesis, yet the underling mechanism remains largely unrevealed. Here, we applied 4D proteomics to screen the lumenogenesis-related proteins and reveal the potentially biological pathways that are involved in lumen inflation during notochord lumen formation in ascidian Ciona savignyi.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Ciona Savignyi

TISSUE(S): Embryo

SUBMITTER: zhuqing wang

LAB HEAD: Bo DONG

PROVIDER: PXD037089 | Pride | 2023-05-10

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	ED131SCB1_STAGEIII_1_Slot2-28_1_17482.zip	Other
	ED131SCB1_STAGEIII_2_Slot2-29_1_17483.zip	Other
	ED131SCB1_STAGEIII_3_Slot2-30_1_17484.zip	Other
	ED131SCB1_STAGEII_1_Slot2-25_1_17478.zip	Other
	ED131SCB1_STAGEII_2_Slot2-26_1_17479.zip	Other

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Publications

Quantitative Phosphoproteomics Reveals the Requirement of DYRK1-Mediated Phosphorylation of Ion Transport- and Cell Junction-Related Proteins for Notochord Lumenogenesis in Ascidian.

Wang Zhuqing Z Ouyang Xiuke X Tan Zicheng Z Yang Likun L Dong Bo B

Cells 20230316 6

The dual-specificity tyrosine phosphorylation-regulated kinase (DYRK1) phosphorylates diverse substrates involved in various cellular processes. Here, we found that blocking the kinase activity of DYRK1 inhibited notochord development and lumenogenesis in ascidian <i>Ciona savignyi</i>. By performing phosphoproteomics in conjunction with notochord-specific proteomics, we identified 1065 notochord-specific phosphoproteins that were present during lumen inflation, of which 428 differentially phosp ...[more]

PMID: 36980262

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