Dataset Information

Phosphorylation Regulatory Networks during honeybee embryogenesis

ABSTRACT: Protein phosphorylation is known to regulate a wide scenario of key cellular processes. However, phosphorylation mediated regulatory networks in honeybee embryogenesis are largely unknown. We identified 6342 phosphosites from 2438 phosphoproteins and predicted 168 kinases in the honeybee embryo. The worker and drone develop similar phosphoproteome architectures and central phosphorylation events during embryogenesis.

ORGANISM(S): Apis Mellifera

SUBMITTER: Yu Fang

PROVIDER: PXD033311 | iProX | Tue Apr 19 00:00:00 BST 2022

REPOSITORIES: iProX

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Publications

Revealing phosphorylation regulatory networks during embryogenesis of honey bee worker and drone (<i>Apis mellifera</i>).

Ma Beibei B Ma Chuan C Li Jianke J Fang Yu Y

Frontiers in cell and developmental biology 20220926

Protein phosphorylation is known to regulate a comprehensive scenario of critical cellular processes. However, phosphorylation-mediated regulatory networks in honey bee embryogenesis are mainly unknown. We identified 6342 phosphosites from 2438 phosphoproteins and predicted 168 kinases in the honey bee embryo. Generally, the worker and drone develop similar phosphoproteome architectures and major phosphorylation events during embryogenesis. In 24 h embryos, protein kinases A play vital roles in ...[more]

PMID: 36225314

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Project description:The honeybee brain is comprised of a nervous system that sufficiently regulates this life transition. Knowledge about how protein phosphorylation functions in regards to the neurobiological activities in the honeybee brain to drive the age-specific labor division is still lacking. Protein phosphorylation, the most common post-translational modification (PTM), is a key switch for rapid on-off control of signaling cascades that regulate cell differentiation and development, enzyme activity and metabolic maintenance in living cells. A fundamental mechanism for regulating signaling network and protein activity is the covalent PTM of serine (Ser), threonine (Thr), and tyrosine (Tyr) residues with phosphate. Fortunately, because of advances in phosphopeptide enrichment and improvements in mass spectrometry (MS) instrumentation and methods, phosphoproteomics has enabled large-scale identification of protein phosphorylation sites and phosphorylation networks in biological samples. Although the proteome has been mapped in the brain of nurse and forager bees, knowledge about age-specific effects of phosphorylation regulation on proteins in the honeybee brain is still lacking. Moreover, information in regards to the honeybee phosphoproteome is also very limited. Only very recently, in-depth phosphoproteomics analyses of protein phosphorylation networks in the hypopharyngealgland of the honeybee have been reported. Although the phosphoproteome analyses during the development of brood and salivary glands has been reported, only very limited proteins were phosphorylated and phosphorylation sites of those phosphoproteins were not assigned. Therefore, a comprehensive characterization of phosphoproteomics and changes in the brains of nurse and forager bees is key to understand the phosphorylation events underlying age-specific physiology to achieve the completion of biological missions in this well-organized social community of the honeybee. Honeybee (A. m. ligustica) colonies used for sampling were raised at the apiary of the Institute of Apicultural Research, Chinese Academy of Agricultural Science, Beijing. Newly emerged (<12 h after emergence) worker bees were marked on their thoraxes and placed back into the colonies to develop and then the marked nurse and forager bees were collected on days 10 and 20, respectively. There were 150 bees sampled from each of the five colonies which have queens at the same age. In brief, for each time point, worker bees were sampled from five colonies, and pooled all samples for further analysis. This procedure was repeated three times, so that we finally ended up with three independent biological replicates per time point, each consisting of 150 honeybees. Then their brains were dissected, and the brain samples were pooled and stored at −80 °C for further analysis. All the colonies were managed with almost identical population, food, and brood during the nectar flow of chaste berry (Vitexnegundo L.) in June.

Project description:Sugarcane (Saccharum spp.) is one of the most important crops for sugar, biofuels and bioenergy production, becoming an important commodity in the world agricultural market for more than 100 countries. In this study, label-free quantitative proteomics and phosphoproteomics analyses were performed to investigate signaling events related to somatic embryo maturation and differentiation in sugarcane. Embryogenic callus (EC) at the multiplication (EC0) and after 14 days (EC14) under maturation were compared. A total of 251 phosphoproteins and 700 proteins were differentially regulated and accumulated, respectively, in the EC14/EC0 comparison. Metabolic pathways analysis showed that proteins and phosphoproteins are enriched in lysine degradation and starch/sucrose metabolism during multiplication, while differentiation of somatic embryo involves the regulation of energetic metabolism, including TCA cycle, oxidative phosphorylation, and carbon metabolism. Multiplication-related phosphoproteins were mainly associated to abscisic acid responses and transcriptional regulation comprising the TOPLESS (TPL), SNF1 kinase homolog 10 (KIN10), SEUSS (SEU), and LEUNIG_HOMOLOG (LUH) proteins. In maturation-related phosphoproteins, the phosphorylation of the proteins light harvesting complex photosystem ii, CURVATURE THYLAKOID 1B, vacuolar proton ATPase A1 and phytochrome interacting factor 3-LIKE 5 is associated to bioenergetic metabolism and carbon fixation. Motif analysis revealed 15 phosphorylation motifs, of which the [D-pS / T-x-D] motif was unique for the phosphopeptides identified during somatic embryo differentiation. Co-expression network analysis of proteins and phosphoproteins revealed the interaction between SNF1-related protein kinase 2 (SnRK2), abscisic acid responsive elements-binding factor 2 (ABF2), and KIN10, indicating the role of these proteins in the embryogenic competence in EC0. The interactions between ubiquitin-conjugating enzyme 5, ubiquitin-conjugating enzyme 35, small ubiquitin-like modifier 1, and histone deacetylase 1 may be involved in post-translational protein modification during the embryo maturation stage. argonaute 1 (AGO1) also interacts with POLTERGEIST (POL) and may integrate gene silencing and regulation of meristem identity during somatic embryo development. These results reveal novel dynamics of protein regulation in somatic embryogenesis and identify new potential players in somatic embryo differentiation and their phosphosites.

Dataset Information

Phosphorylation Regulatory Networks during honeybee embryogenesis

Publications

Revealing phosphorylation regulatory networks during embryogenesis of honey bee worker and drone (<i>Apis mellifera</i>).

Similar Datasets

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