ArticleThe Journal of experimental biology2012
A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation.
Article in The Journal of experimental biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Assessing structure-function impacts on Vitellogenin by leveraging allelic variant found in honey bee subspeciesiScience · 2025Article
- Cryo-EM structure of native honey bee vitellogenin.Nature communications · 2025Article
- Resolving the zinc binding capacity of honey bee vitellogenin and locating its putative binding sites.Insect molecular biology · 2022Article
- Molecular Characterization of Vitellogenin and Its Receptor inInternational journal of molecular sciences · 2022Article
- Balanced Force Field ff03CMAP Improving the Dynamics Conformation Sampling of Phosphorylation Site.International journal of molecular sciences · 2022Article
- Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites.Protein science : a publication of the Protein Society · 2022Article
- How Honey Bee Vitellogenin Holds Lipid Cargo: A Role for the C-Terminal.Frontiers in molecular biosciences · 2022Article
- Structure prediction of honey bee vitellogenin: a multi-domain protein important for insect immunity.FEBS open bio · 2022Article
- Nuclear translocation of vitellogenin in the honey bee (Apidologie · 2022Article
- Potentially adaptive SARS-CoV-2 mutations discovered with novel spatiotemporal and explainable AI models.Genome biology · 2020Article
- Biopanning of allergens from wasp sting patients.Bioscience reports · 2018Article
- The unique N-terminal sequence of the BKCa channel α-subunit determines its modulation by β-subunits.PloS one · 2017Article
- Ancient Duplications Have Led to Functional Divergence of Vitellogenin-Like Genes Potentially Involved in Inflammation and Oxidative Stress in Honey Bees.Genome biology and evolution · 2016Article
- The intrinsic disorder alphabet. III. Dual personality of serine.Intrinsically disordered proteins · 2015Review
- Vitellogenin recognizes cell damage through membrane binding and shields living cells from reactive oxygen species.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Vitellogenin (Vg) is an egg-yolk precursor protein in most oviparous species. In honeybee (Apis mellifera), the protein (AmVg) also affects social behavior and life-span plasticity. Despite its manifold functions, the AmVg molecule remains poorly understood. The subject of our structure-oriented AmVg study is its polyserine tract - a little-investigated repetitive protein segment mostly found in insects. We previously reported that AmVg is tissue specifically cleaved in the vicinity of this tract. Here, we show that, despite its potential for an open, disordered structure, AmVg is unexpectedly resistant to trypsin/chymotrypsin digestion at the tract. Our findings suggest that multiple phosphorylation plays a role in this resilience. Sequence variation is highly pronounced at the polyserine region in insect Vgs. We demonstrate that sequence differences in this region can lead to structural variation, as NMR and circular dichroism (CD) evidence assign different conformational propensities to polyserine peptides from the honeybee and the jewel wasp Nasonia vitripennis; the former is extended and disordered and the latter more compact and helical. CD analysis of the polyserine region of bumblebee Bombus ignitus and wasp Pimpla nipponica supports a random coil structure in these species. The spectroscopic results strengthen our model of the AmVg polyserine tract as a flexible domain linker shielded by phosphorylation.
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