Dataset Information

Integrative proteomics and phosphoproteomics analysis of the rat adenohypophysis after GnRH treatment

ABSTRACT: Quantitative protein proteomics by TMT labeling and phosphorylation enrichment techniques and high-resolution liquid chromatography-mass spectrometry

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Adenohypophysis

SUBMITTER: Wenzhi Ren

LAB HEAD: Tian Wang

PROVIDER: PXD036177 | Pride | 2023-03-11

REPOSITORIES: Pride

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Integrative Proteomics and Phosphoproteomics Analysis of the Rat Adenohypophysis after GnRH Treatment.

Wang Tian T Wang Hao-Qi HQ Yuan Bao B Zhao Guo-Kun GK Ma Yi-Ran YR Zhao Pei-Sen PS Xie Wen-Yin WY Gao Fei F Gao Wei W Ren Wen-Zhi WZ

International journal of molecular sciences 20230207 4

The regulation of mammalian reproductive activity is tightly dependent on the HPG axis crosstalk, in which several reproductive hormones play important roles. Among them, the physiological functions of gonadotropins are gradually being uncovered. However, the mechanisms by which GnRH regulates FSH synthesis and secretion still need to be more extensively and deeply explored. With the gradual completion of the human genome project, proteomes have become extremely important in the fields of human ...[more]

PMID: 36834752

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Project description:N-glycosylation is an important posttranslational modification in all eukaryotes, but little is known about the N-glycoproteomes in microalgal systems. Here, N-glycoproteome of the model diatom Phaeodactylum tricornutum was unveiled. Totally, 893 different N-glycosylated sites from 649 proteins were identified from P. tricornutum. The new synthesized N-glycans were principally transferred to asparagine residues within the conserved N-X-S/T (where X is a residue other than proline) sequence of nascent polypeptide chains. Functional annotation of N-glycosylated proteins showed that 70% N-glycoproteins were involved in vesicular transport and posttranslational modification, protein turnover, chaperones, indicating the N-glycosylation was important for these functions. Of the all identified N-glycoproteins 45.3% were predicted to localize on chloroplast, which implied the widespread regulatory role of N-glycosylation in chloroplast. Furthermore, the enrichment results of N-glycoproteins indicated that compared to ‘Cellular component’ and ‘Biological process’ categories proteins related with the ‘Molecular function’ category were more prone to be N-glycosylated. And it was speculated that N-glycosylation played a vital regulatory role in catalytic activity of enzymes and metabolism processes of many small molecules. 47% of all enriched proteins were related with metabolic pathways. The functional annotation and enrichment of N-glycoproteins suggested that N-glycoproteins participated in a variety of important metabolic pathways and perform different functions in P. tricornutum. 12 proteins involved in the ER quality control mechanism and ER- associated degradation pathway were identified as N-glycosylated proteins, indicating that the N-glycosylated modification was important for their functions in the protein N-glycosylation pathway. Additionally, some interacted glycoproteins were classified from this study, which provided valuable information for studying the functions of these glycoproteins. In the study, the identification of N-glycosylation on nascent proteins expands our understanding of this PTM at a proteomics scale and may facilitate the elucidation of the precise function of proteins in this model diatom.

			Action	DRS
	F9535PRM1_GnRH_1.raw	Raw
	F9535PRM1_GnRH_2.raw	Raw
	F9535PRM1_GnRH_3.raw	Raw
	F9535PRM1_NC_1.raw	Raw
	F9535PRM1_NC_2.raw	Raw