Modified Proteome Analysis

Importance of phosphorylation

Protein phosphorylation is a very important and widely present post-translational modification regulation method in prokaryotes and eukaryotes. It is involved in cell proliferation, development, differentiation, apoptosis, cytoskeleton regulation, neural activity, muscle contraction, metabolism, and tumor occurrence and so on. It plays a biological regulatory role in many biological cell functions. The study of phosphorylated proteome can help analyze the complex physiological and pathological processes of organisms.

Through biological information analysis of phosphorylation data, such as using Skyline20, Comet21, DIA-Umpire24 and other biological analysis software, in addition to relative quantification of post-translational phosphorylation in the sample, screening of differential phosphorylation sites and differentially expressed phosphorylated proteins, unknown new phosphorylation sites and phosphorylated proteins can also be discovered.

Fig 1. Phosphoproteome Oscillations inthe Mouse Livers. (Maria S. et al. 2017)

Application Field

Protein phosphorylation data analysis can be applied to the following fields, but not limited to the following fields

Research on the mechanism of disease occurrence and development

Disease marker screening

Drug target research

Health research

Reference

1. Maria S. et al.,Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology [J], Cell Metabolism, 2017. 25, 1–10.

Importance of Acetylation

Acetylation modification is an evolutionarily conserved reversible post-translational modification (PTM), which exists in both prokaryotes and eukaryotes. Acetylation involves key cellular processes related to physiology and disease, such as the impact on gene transcription, DNA damage repair, cell division cycle, signal transduction, protein folding, autophagy and metabolism. At the same time, acetylation modification affects protein functions through a variety of mechanisms, including regulation of protein stability, enzyme activity, subcellular localization, crosstalk with other post-translational modifications, and regulation of protein-protein and protein-DNA interactions. The study of acetylated proteome can help analyze the complex and diverse physiological and pathological processes of life.

Through biological information analysis of phosphorylation data, such as using MaxQuant and other biological analysis software, in addition to relative quantification of post-translational acetylation in the sample, screening of differential acetylation sites and differentially expressed acetylation proteins, unknown new acetylation sites and acetylation proteins can also be discovered.

Fig 1. Research process of lysine acetylation of Trichoderma rubrum. (Xu X, et al. 2018)

Application Field

Protein acetylation research can be used for basic research in the following areas.

Research on molecular mechanisms such as cell differentiation and cellular immunity

Mechanism of disease occurrence and development

Medication mechanism

Discovery of therapeutic targets

Reference

1. Xu X, et al. The first whole-cell proteome- and lysine-acetylome-based comparison between Trichophyton rubrum conidial and mycelial stages[J]. Journal of Proteome Research, 2018 :acs. jproteome. 7b00793.

Importance of Glycosylation

Glycosylation is an important post-translational modification of proteins. It plays an extremely important role in the structure and function of proteins. Its most important function is to properly fold peptides synthesized in the endoplasmic reticulum. According to the different connection modes of sugar chains and peptide chains, protein glycosylation can be divided into N-glycosylation and O-glycosylation. Glycosylation regulates the location, function, activity, lifespan and diversity of proteins in tissues and cells, and participates in various important life activities including cell recognition, differentiation, development, signal transduction, and immune response.

Use GlycoMod and other bioinformatics analysis software to analyze protein glycosylation data, and perform qualitative and quantitative analysis of protein glycosylation modification status to obtain protein glycosylation modification differences under different processing or different physiological and pathological conditions, which will lay a foundation for subsequent research data basis. Studies have shown that various diseases, such as tumors, neurodegenerative diseases, cardiovascular diseases, metabolic diseases, immune diseases and infectious diseases, are accompanied by abnormal protein glycosylation.

Fig 1. MS/MS spectra of the major glycoforms of glycopeptides covering six N-glycosylation sites.
(Yagi H , et al. 2018)

Application Field

Protein glycosylation research can be used for basic research in the following areas.

Research on the mechanism of disease occurrence and development

Disease marker screening

Drug target research

Health research

Reference

1. Yagi H , et al. Site-specific N-glycosylation analysis of soluble Fcγ receptor IIIb in human serum[J]. Scientific Reports, 2018, 8(1):2719.

Importance of Ubiquitination

Ubiquitination modification is an important post-translational modification, which plays a very important role in protein localization, metabolism, function regulation and degradation. At the same time, it also participates in cell cycle, proliferation, apoptosis, differentiation, and metastasis, gene expression, transcription regulation, signal transmission, damage repair, inflammation and immunity and other life activities regulation. Therefore, ubiquitination modification has almost participated in all life activities of eukaryotes.

Use GlycoMod and other bioinformatics analysis software to analyze protein abiquitination data, and perform qualitative and quantitative analysis of protein abiquitination modification status to obtain protein abiquitination modification differences under different processing or different physiological and pathological conditions, which will lay a foundation for subsequent research data basis. Studies have shown that ubiquitination is closely related to the onset of tumors, neurodegenerative diseases, muscular dystrophy, immune diseases, cardiovascular diseases and metabolic syndrome. In addition, the study of ubiquitination modification has great potential application value in improving plants' response to stress environments.

Fig 1. Application of protein ubiquitination modification analysis in the study of rice resistance mechanism. (Li X M , et al. 2015)

Application Field

Protein ubiquitination research can be used for basic research in the following areas, but not limited to the following research areas.

Disease research and treatment

Medication mechanism

Research on Plant Resistance

Reference

1. Li X M , et al. Natural alleles of a proteasome α2 subunit gene contribute to thermotolerance and adaptation of African rice[J]. Nature Genetics, 2015, 47(7):827-33.