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SNX18 tubulates recycling endosomes for autophagosome biogenesis
Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
2013 (English)In: Autophagy, ISSN 1554-8627, E-ISSN 1554-8635, ISSN 1554-8635 (online), Vol. 9, no 10, 1639-1641 p.Article in journal (Refereed) Published
Abstract [en]

The role of membrane remodeling and phosphoinositide-binding proteins in autophagy remains elusive. PX domain proteins bind phosphoinositides and participate in membrane remodeling and trafficking events and we therefore hypothesized that one or several PX domain proteins are involved in autophagy. Indeed, the PX-BAR protein SNX18 was identified as a positive regulator of autophagosome formation using an image-based siRNA screen. We show that SNX18 interacts with ATG16L1 and LC3, and functions downstream of ATG14 and the class III PtdIns3K complex in autophagosome formation. SNX18 facilitates recruitment of ATG16L1 to perinuclear recycling endosomes, and its overexpression leads to tubulation of ATG16L1- and LC3-positive membranes. We propose that SNX18 promotes LC3 lipidation and tubulation of recycling endosomes to provide membrane for phagophore expansion.

Place, publisher, year, edition, pages
Landes Bioscience , 2013. Vol. 9, no 10, 1639-1641 p.
Keyword [en]
SNX18, recycling endosomes, PX-BAR protein, autophagosome formation, ATG16L1, RAB11
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:umu:diva-82408DOI: 10.4161/auto.26124PubMedID: 24113029OAI: oai:DiVA.org:umu-82408DiVA: diva2:661087
Available from: 2013-10-31 Created: 2013-10-31 Last updated: 2017-12-06Bibliographically approved

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Carlsson, Sven R

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