title: The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella.
abstract: Salmonella develops into resident bacteria in epithelial cells, and the autophagic machinery (Atg) is thought to play an important role in this process. In this paper, we show that an autophagosome-like double-membrane structure surrounds the Salmonella still residing within the Salmonella-containing vacuole (SCV). This double membrane is defective in Atg9L1- and FAK family-interacting protein of 200 kDa (FIP200)-deficient cells. Atg9L1 and FIP200 are important for autophagy-specific recruitment of the phosphatidylinositol 3-kinase (PI3K) complex. However, in the absence of Atg9L1, FIP200, and the PI3K complex, LC3 and its E3-like enzyme, the Atg16L complex, are still recruited to Salmonella. We propose that the LC3 system is recruited through a mechanism that is independent of isolation membrane generation.
authors.affiliation: Laboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
authors.forename: Shun
authors.initials: S
authors.lastname: Kageyama
authors.forename: Hiroko
authors.initials: H
authors.lastname: Omori
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Saitoh
authors.forename: Takefumi
authors.initials: T
authors.lastname: Sone
authors.forename: Jun-Lin
authors.initials: JL
authors.lastname: Guan
authors.forename: Shizuo
authors.initials: S
authors.lastname: Akira
authors.forename: Fumio
authors.initials: F
authors.lastname: Imamoto
authors.forename: Takeshi
authors.initials: T
authors.lastname: Noda
authors.forename: Tamotsu
authors.initials: T
authors.lastname: Yoshimori
mesh_terms: D000818:Animals; D001343:Autophagy / Q000502:physiology*; D000071183:Autophagy-Related Proteins; D051417:Focal Adhesion Kinase 1 / Q000378:metabolism; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D041681:NIH 3T3 Cells; D010588:Phagosomes / Q000378:metabolism; D019869:Phosphatidylinositol 3-Kinases / Q000378:metabolism; D012475:Salmonella / Q000166:cytology* / Q000378:metabolism; D012480:Salmonella Infections / Q000378:metabolism* / Q000473:pathology; D014617:Vacuoles / Q000378:metabolism; D033921:Vesicular Transport Proteins
chemical_list: D000071183:Autophagy-Related Proteins; D051417:Focal Adhesion Kinase 1; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D019869:Phosphatidylinositol 3-Kinases; D033921:Vesicular Transport Proteins; C549015:Atg9A protein, mouse; C480860:Map1lc3b protein, mouse; C428743:Rb1cc1 protein, mouse; C496051:Ptk2 protein, mouse