A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling

Membrane protein recycling systems are essential for maintenance of the endosome-lysosome system. In yeast, retromer and Snx4 coat complexes are recruited to the endosomal surface, where they recognize cargos. They sort cargo and deform the membrane into recycling tubules that bud from the endosome...

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Autores principales:	Sho W Suzuki, Akihiko Oishi, Nadia Nikulin, Jeff R Jorgensen, Matthew G Baile, Scott D Emr
Formato:	article
Lenguaje:	EN
Publicado:	eLife Sciences Publications Ltd 2021
Materias:	retromer SNX8 dynamin endosome BAR domain Medicine R Science Q Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/a9f1cb1fcb794ed1845a88c49cb1fc83
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id	oai:doaj.org-article:a9f1cb1fcb794ed1845a88c49cb1fc83
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spelling	oai:doaj.org-article:a9f1cb1fcb794ed1845a88c49cb1fc832021-11-30T10:06:01ZA PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling10.7554/eLife.698832050-084Xe69883https://doaj.org/article/a9f1cb1fcb794ed1845a88c49cb1fc832021-09-01T00:00:00Zhttps://elifesciences.org/articles/69883https://doaj.org/toc/2050-084XMembrane protein recycling systems are essential for maintenance of the endosome-lysosome system. In yeast, retromer and Snx4 coat complexes are recruited to the endosomal surface, where they recognize cargos. They sort cargo and deform the membrane into recycling tubules that bud from the endosome and target to the Golgi. Here, we reveal that the SNX-BAR protein, Mvp1, mediates an endosomal recycling pathway that is mechanistically distinct from the retromer and Snx4 pathways. Mvp1 deforms the endosomal membrane and sorts cargos containing a specific sorting motif into a membrane tubule. Subsequently, Mvp1 recruits the dynamin-like GTPase Vps1 to catalyze membrane scission and release of the recycling tubule. Similarly, SNX8, the human homolog of Mvp1, which has been also implicated in Alzheimer’s disease, mediates formation of an endosomal recycling tubule. Thus, we present evidence for a novel endosomal retrieval pathway that is conserved from yeast to humans.Sho W SuzukiAkihiko OishiNadia NikulinJeff R JorgensenMatthew G BaileScott D EmreLife Sciences Publications LtdarticleretromerSNX8dynaminendosomeBAR domainMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	retromer SNX8 dynamin endosome BAR domain Medicine R Science Q Biology (General) QH301-705.5
spellingShingle	retromer SNX8 dynamin endosome BAR domain Medicine R Science Q Biology (General) QH301-705.5 Sho W Suzuki Akihiko Oishi Nadia Nikulin Jeff R Jorgensen Matthew G Baile Scott D Emr A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling
description	Membrane protein recycling systems are essential for maintenance of the endosome-lysosome system. In yeast, retromer and Snx4 coat complexes are recruited to the endosomal surface, where they recognize cargos. They sort cargo and deform the membrane into recycling tubules that bud from the endosome and target to the Golgi. Here, we reveal that the SNX-BAR protein, Mvp1, mediates an endosomal recycling pathway that is mechanistically distinct from the retromer and Snx4 pathways. Mvp1 deforms the endosomal membrane and sorts cargos containing a specific sorting motif into a membrane tubule. Subsequently, Mvp1 recruits the dynamin-like GTPase Vps1 to catalyze membrane scission and release of the recycling tubule. Similarly, SNX8, the human homolog of Mvp1, which has been also implicated in Alzheimer’s disease, mediates formation of an endosomal recycling tubule. Thus, we present evidence for a novel endosomal retrieval pathway that is conserved from yeast to humans.
format	article
author	Sho W Suzuki Akihiko Oishi Nadia Nikulin Jeff R Jorgensen Matthew G Baile Scott D Emr
author_facet	Sho W Suzuki Akihiko Oishi Nadia Nikulin Jeff R Jorgensen Matthew G Baile Scott D Emr
author_sort	Sho W Suzuki
title	A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling
title_short	A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling
title_full	A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling
title_fullStr	A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling
title_full_unstemmed	A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling
title_sort	px-bar protein mvp1/snx8 and a dynamin-like gtpase vps1 drive endosomal recycling
publisher	eLife Sciences Publications Ltd
publishDate	2021
url	https://doaj.org/article/a9f1cb1fcb794ed1845a88c49cb1fc83
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A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling

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