The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage

Abstract 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....

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Autores principales:	Surya Banerjee, Christine Woods, Micheal Burnett, Scarlet J. Park, William W. Ja, Jennifer Curtiss
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/08b56112c1ea4be0bab0722457235db9
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spelling	oai:doaj.org-article:08b56112c1ea4be0bab0722457235db92021-12-02T15:23:47ZThe Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage10.1038/s41598-021-81165-z2045-2322https://doaj.org/article/08b56112c1ea4be0bab0722457235db92021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-81165-zhttps://doaj.org/toc/2045-2322Abstract 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.Surya BanerjeeChristine WoodsMicheal BurnettScarlet J. ParkWilliam W. JaJennifer CurtissNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-18 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Surya Banerjee Christine Woods Micheal Burnett Scarlet J. Park William W. Ja Jennifer Curtiss The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage
description	Abstract 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.
format	article
author	Surya Banerjee Christine Woods Micheal Burnett Scarlet J. Park William W. Ja Jennifer Curtiss
author_facet	Surya Banerjee Christine Woods Micheal Burnett Scarlet J. Park William W. Ja Jennifer Curtiss
author_sort	Surya Banerjee
title	The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage
title_short	The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage
title_full	The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage
title_fullStr	The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage
title_full_unstemmed	The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage
title_sort	drosophila melanogaster neprilysin nepl15 is involved in lipid and carbohydrate storage
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/08b56112c1ea4be0bab0722457235db9
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The Drosophila melanogaster Neprilysin Nepl15 is involved in lipid and carbohydrate storage

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