Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein

Abstract Membrane-bound sialidase Neu3 is involved in the catabolism of glycoconjugates, and plays crucial roles in numerous biological processes. Since the mechanism of its association with membranes is still not completely understood, the aim of this work was to provide further information regardi...

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Autores principales:	Macarena Rodriguez-Walker, Jose L. Daniotti
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0e3f1193fc3844af850a106d04672979
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spelling	oai:doaj.org-article:0e3f1193fc3844af850a106d046729792021-12-02T16:06:42ZHuman Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein10.1038/s41598-017-04488-w2045-2322https://doaj.org/article/0e3f1193fc3844af850a106d046729792017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04488-whttps://doaj.org/toc/2045-2322Abstract Membrane-bound sialidase Neu3 is involved in the catabolism of glycoconjugates, and plays crucial roles in numerous biological processes. Since the mechanism of its association with membranes is still not completely understood, the aim of this work was to provide further information regarding this aspect. Human Neu3 was found to be associated with the plasma membrane and endomembranes, and it was not released from the lipid bilayer under conditions that typically release peripheral membrane proteins. By different experimental approaches, we demonstrated that its C-terminus is exposed to the cytosol while another portion of the protein is exposed to the extracellular space, suggesting that Neu3 possesses the features of a transmembrane protein. However, in silico analysis and homology modeling predicted that the sialidase does not contain any α-helical transmembrane segment and shares the same β-propeller fold typical of viral and bacterial sialidases. Additionally, we found that Neu3 is S-acylated. Since this post-translational modification is restricted to the cytosolic side of membranes, this finding strongly supports the idea that Neu3 may contain a cytosolic-exposed domain. Although it remains to be determined exactly how this sialidase crosses the lipid bilayer, this study provides new insights about membrane association and topology of Neu3.Macarena Rodriguez-WalkerJose L. DaniottiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Macarena Rodriguez-Walker Jose L. Daniotti Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein
description	Abstract Membrane-bound sialidase Neu3 is involved in the catabolism of glycoconjugates, and plays crucial roles in numerous biological processes. Since the mechanism of its association with membranes is still not completely understood, the aim of this work was to provide further information regarding this aspect. Human Neu3 was found to be associated with the plasma membrane and endomembranes, and it was not released from the lipid bilayer under conditions that typically release peripheral membrane proteins. By different experimental approaches, we demonstrated that its C-terminus is exposed to the cytosol while another portion of the protein is exposed to the extracellular space, suggesting that Neu3 possesses the features of a transmembrane protein. However, in silico analysis and homology modeling predicted that the sialidase does not contain any α-helical transmembrane segment and shares the same β-propeller fold typical of viral and bacterial sialidases. Additionally, we found that Neu3 is S-acylated. Since this post-translational modification is restricted to the cytosolic side of membranes, this finding strongly supports the idea that Neu3 may contain a cytosolic-exposed domain. Although it remains to be determined exactly how this sialidase crosses the lipid bilayer, this study provides new insights about membrane association and topology of Neu3.
format	article
author	Macarena Rodriguez-Walker Jose L. Daniotti
author_facet	Macarena Rodriguez-Walker Jose L. Daniotti
author_sort	Macarena Rodriguez-Walker
title	Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein
title_short	Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein
title_full	Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein
title_fullStr	Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein
title_full_unstemmed	Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein
title_sort	human sialidase neu3 is s-acylated and behaves like an integral membrane protein
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/0e3f1193fc3844af850a106d04672979
work_keys_str_mv	AT macarenarodriguezwalker humansialidaseneu3issacylatedandbehaveslikeanintegralmembraneprotein AT joseldaniotti humansialidaseneu3issacylatedandbehaveslikeanintegralmembraneprotein
_version_	1718384885014462464

Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein

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