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1.
Genes Brain Behav ; 18(1): e12509, 2019 01.
Article in English | MEDLINE | ID: mdl-30094933

ABSTRACT

Social interactions can be divided into two categories, affiliative and agonistic. How neurogenomic responses reflect these opposing valences is a central question in the biological embedding of experience. To address this question, we exposed honey bees to a queen larva, which evokes nursing, an affiliative alloparenting interaction, and measured the transcriptomic response of the mushroom body brain region at different times after exposure. Hundreds of genes were differentially expressed at distinct time points, revealing a dynamic temporal patterning of the response. Comparing these results to our previously published research on agonistic aggressive interactions, we found both shared and unique transcriptomic responses to each interaction. The commonly responding gene set was enriched for nuclear receptor signaling, the set specific to nursing was enriched for olfaction and neuron differentiation, and the set enriched for aggression was enriched for cytoskeleton, metabolism, and chromosome organization. Whole brain histone profiling after the affiliative interaction revealed few changes in chromatin accessibility, suggesting that the transcriptomic changes derive from already accessible areas of the genome. Although only one stimulus of each type was studied, we suggest that elements of the observed transcriptomic responses reflect molecular encoding of stimulus valence, thus priming individuals for future encounters. This hypothesis is supported by behavioral analyses showing that bees responding to either the affiliative or agonistic stimulus exhibited a higher probability of repeating the same behavior but a lower probability of performing the opposite behavior. These findings add to our understanding of the biological embedding at the molecular level.


Subject(s)
Agonistic Behavior , Bees/genetics , Cooperative Behavior , Transcriptome , Animals , Bees/physiology , Brain/metabolism , Brain/physiology , Learning
2.
Arch Biochem Biophys ; 616: 20-29, 2017 02 15.
Article in English | MEDLINE | ID: mdl-28065721

ABSTRACT

Key residues and binding mechanisms of PGE1 and PGE2 on prostanoid receptors are poorly understood due to the lack of X-ray structures for the receptors. We constructed a human EP3 (hEP3) model through integrative homology modeling using the X-ray structure of the ß2-adrenergic receptor transmembrane domain and NMR structures of the thromboxane A2 receptor extracellular loops. PGE1 and PGE2 docking into the hEP3 model showed differing configurations within the extracellular ligand recognition site. While PGE2 could form possible binding contact with S211, PGE1 is unable to form similar contacts. Therefore, S211 could be the critical residue for PGE2 recognition, but is not a significant for PGE1. This prediction was confirmed using HEK293 cells transfected with hEP3 S211L cDNA. The S211L cells lost PGE2 binding and signaling. Interestingly, the S211L cells retained PGE1-mediated signaling. It indicates that S211 within the second extracellular loop is a key residue involved in turning down PGE2 signaling. Our study provided information that S211L within EP3 is the key residue to distinguish PGE1 and PGE2 binding to mediate diverse biological functions at the initial recognition step. The S211L mutant could be used as a model for studying the binding mechanism and signaling pathway specifically mediated by PGE1.


Subject(s)
Alprostadil/chemistry , Dinoprostone/chemistry , Receptors, Prostaglandin E, EP3 Subtype/chemistry , Receptors, Prostaglandin E, EP3 Subtype/genetics , Binding Sites , Calcium Signaling , Crystallography, X-Ray , DNA, Complementary/chemistry , HEK293 Cells , Humans , Ligands , Magnetic Resonance Spectroscopy , Mutagenesis, Site-Directed , Mutation , Protein Binding , Protein Domains , Receptors, Adrenergic, beta-2/chemistry , Recombinant Proteins/chemistry , Signal Transduction
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