Abstract
The first genomic and chemical characterization of fruit fly neuropeptides outside Drosophila melanogaster provides insights into the evolution of the neuropeptidome in this genus.
Highlights
Neuropeptides comprise the most diverse group of neuronal signaling molecules
The epitracheal cells (Inka cells) are endocrine glands along the trachea. These tissues represent a rich source of neuropeptides: their peptidome contains about half of all known D. melanogaster neuropeptides [35,36]
To biochemically assess whether the neuropeptides are expressed and processed as predicted, we directly profiled these neurohemal organs in D. sechellia, D. pseudoobscura, D. mojavensis and D. virilis
Summary
Neuropeptides comprise the most diverse group of neuronal signaling molecules They often occur as multiple sequence-related copies within single precursors (the prepropeptides). According to a classic model of molecular evolution [6], this is because a duplicated peptide sequence may be able to escape from natural selection and drift neutrally [7] if its original function is maintained by its paralog. The mutations accumulating in the 'escaped' peptide sequence may lead to nonfunctionalization, subfunctionalization or neofunctionalization by acquisition of new features such as altered half-life, altered receptor binding kinetics, altered tissue expression patterns (for example, neuropeptides of the NPY family or the POMC prepropeptide [1,8]) or receptor specificities by peptide-receptor co-evolution [9,10]. If the increased amount of peptides resulting from the duplication is beneficial, the duplicated peptide may immediately increase Darwinian fitness prior to an accumulation of sequence mutations ('more-ofthe-same') [10,11]
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