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Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion

Nature structural & molecular biology, 2020-12, Vol.27 (12), p.1185-1193 [Peer Reviewed Journal]

The Author(s), under exclusive licence to Springer Nature America, Inc. 2020. ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-020-00518-w ;PMID: 33106658

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Title:
Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion
Author: Matoba, Kazuaki ; Kotani, Tetsuya ; Tsutsumi, Akihisa ; Tsuji, Takuma ; Mori, Takaharu ; Noshiro, Daisuke ; Sugita, Yuji ; Nomura, Norimichi ; Iwata, So ; Ohsumi, Yoshinori ; Fujimoto, Toyoshi ; Nakatogawa, Hitoshi ; Kikkawa, Masahide ; Noda, Nobuo N
Subjects: Autophagosomes - chemistry ; Autophagosomes - metabolism ; Autophagy ; Autophagy-Related Proteins - chemistry ; Autophagy-Related Proteins - genetics ; Autophagy-Related Proteins - metabolism ; Binding Sites ; Biological Transport ; Cryoelectron Microscopy ; Endoplasmic reticulum ; Expansion ; Gene Expression ; Green Fluorescent Proteins - chemistry ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; Humans ; Lipid Bilayers - chemistry ; Lipid Bilayers - metabolism ; Lipids ; Liposomes ; Luminescent Proteins - genetics ; Luminescent Proteins - metabolism ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Models, Molecular ; Mutation ; Phagocytosis ; Phospholipids ; Phospholipids - chemistry ; Phospholipids - metabolism ; Pores ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Proteolipids - chemistry ; Proteolipids - metabolism ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Red Fluorescent Protein ; Saccharomyces cerevisiae - chemistry ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Trimers ; Vesicular Transport Proteins - chemistry ; Vesicular Transport Proteins - genetics ; Vesicular Transport Proteins - metabolism ; Yeast ; Yeasts
Is Part Of: Nature structural & molecular biology, 2020-12, Vol.27 (12), p.1185-1193
Description: The molecular function of Atg9, the sole transmembrane protein in the autophagosome-forming machinery, remains unknown. Atg9 colocalizes with Atg2 at the expanding edge of the isolation membrane (IM), where Atg2 receives phospholipids from the endoplasmic reticulum (ER). Here we report that yeast and human Atg9 are lipid scramblases that translocate phospholipids between outer and inner leaflets of liposomes in vitro. Cryo-EM of fission yeast Atg9 reveals a homotrimer, with two connected pores forming a path between the two membrane leaflets: one pore, located at a protomer, opens laterally to the cytoplasmic leaflet; the other, at the trimer center, traverses the membrane vertically. Mutation of residues lining the pores impaired IM expansion and autophagy activity in yeast and abolished Atg9's ability to transport phospholipids between liposome leaflets. These results suggest that phospholipids delivered by Atg2 are translocated from the cytoplasmic to the luminal leaflet by Atg9, thereby driving autophagosomal membrane expansion.
Publisher: United States: Nature Publishing Group
Language: English
Identifier: ISSN: 1545-9993
EISSN: 1545-9985
DOI: 10.1038/s41594-020-00518-w
PMID: 33106658
Source: MEDLINE
ProQuest Central

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Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion

The Author(s), under exclusive licence to Springer Nature America, Inc. 2020. ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-020-00518-w ;PMID: 33106658

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