ArticleFrontiers in cell and developmental biology2022
Revealing phosphorylation regulatory networks during embryogenesis of honey bee worker and drone (
Article in Frontiers in cell and developmental biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 6 citations in OpenAlex.
- Proteome Unravels Mechanism Differences in Embryogenesis Between Honey Bee Drone and Worker (Apis mellifera L.).Molecular & cellular proteomics : MCP · 2026Article
- Time-series transcriptomics and alternative splicing analysis of embryonic development of the asian honeybee (Frontiers in genetics · 2025Article
- Based proteomics analyses reveal response mechanisms of Apis mellifera (Hymenoptera: Apidae) against the heat stress.Journal of insect science (Online) · 2024Article
- Proteome-metabolome profiling of wax gland complex reveals functional changes in honeybee,iScience · 2024Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
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 regulating cell proliferation and blastoderm formation. At 48-72 h, kinase subfamily dual-specificity tyrosine-regulated kinase, cyclin-dependent kinase (CDK), and induced pathways related to protein synthesis and morphogenesis suggest the centrality to enhance the germ layer development, organogenesis, and dorsal closure. Notably, workers and drones formulated distinct phosphoproteome signatures. For 24 h embryos, the highly phosphorylated serine/threonine-protein kinase minibrain, microtubule-associated serine/threonine-protein kinase 2 (MAST2), and phosphorylation of mitogen-activated protein kinase 3 (MAPK3) at Thr
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