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The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage
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The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage
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Journal Article
The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage
2021
Overview
The prototypical M13 peptidase, human Neprilysin, functions as a transmembrane “ectoenzyme” that cleaves neuropeptides that regulate e.g. glucose metabolism, and has been linked to type 2 diabetes. The M13 family has undergone a remarkable, and conserved, expansion in the
Drosophila
genus. Here, we describe the function of
Drosophila melanogaster
Neprilysin-like 15 (Nepl15). Nepl15 is likely to be a secreted protein, rather than a transmembrane protein. Nepl15 has changes in critical catalytic residues that are conserved across the Drosophila genus and likely renders the Nepl15 protein catalytically inactive. Nevertheless, a knockout of the
Nepl15
gene reveals a reduction in triglyceride and glycogen storage, with the effects likely occurring during the larval feeding period. Conversely, flies overexpressing
Nepl15
store more triglycerides and glycogen. Protein modeling suggests that Nepl15 is able to bind and sequester peptide targets of catalytically active
Drosophila
M13 family members, peptides that are conserved in humans and
Drosophila
, potentially providing a novel mechanism for regulating the activity of neuropeptides in the context of lipid and carbohydrate homeostasis.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
