Cited by 175Autophagy in Disease and TherapyCellular transport and secretionATP Synthase and ATPases Research

The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella

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Kageyama, Shun, Omori, Hiroko, Saitoh, Tatsuya, Sone, Takefumi, Guan, Jun-Lin, Akira, Shizuo, Imamoto, Fumio, Noda, Takeshi +1 more·2011·Molecular Biology of the Cell

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.

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Crossref · 10.1091/mbc.e10-11-0893

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  • Infection of phagocytic neutrophils or non-phagocytic MEF cells expressing GFP-LC3 by Salmonella typhimurium resulted in recruitment of GFP-LC3 to bacteria-containing phagosomes.

    “Similarly, infection of either phagocytic neutrophils or non-phagocytic mouse embryonic fibroblast (MEF) cells, each expressing GFP-LC3, by Salmonella typhimurium also resulted in the recruitment of GFP-LC3 to bacteria-containing phagosomes [14,33].”

    From LC3-Associated Phagocytosis (LAP): Connections with Host Autophagy (2012) · cites this paper as [33]

    The Results section, “LC3 associates with S. typhimurium through an LC3-lipidation reaction” (page unavailable), reports that GFP-LC3 surrounded S. typhimurium in infected MEFs. Our copy does not establish the corresponding finding in neutrophils or identify the LC3-positive structures as bacteria-containing phagosomes. (LLM, conf=0.87)

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Authors
Kageyama, S., Omori, H., Saitoh, T., Sone, T., Guan, J.-L., Akira, S., Imamoto, F., Noda, T., & Yoshimori, T.
Affiliations
  • The University of Osaka (JP)
  • Research Institute for Microbial Diseases, The University of Osaka (JP)
  • Immunology Frontier Research Center, The University of Osaka (JP)
  • University of Michigan (US)
Corresponding author
Noda, Takeshi
Venue
Molecular Biology of the Cell
Published
2011-07
Volume
22
Issue
13
Pages
2290-2300
ISSN
  • 1059-1524 (ISSN-L)
  • 1939-4586
OpenAlex
W2061541746
Cited by
175
References
52
Citations by year
2026: 5 · 2025: 7 · 2024: 5 · 2023: 5 · 2022: 7 · 2021: 8 · 2020: 9 · 2019: 15 · 2018: 3 · 2017: 13 · 2016: 16 · 2015: 7 · 2014: 26 · 2013: 19 · 2012: 26
FWCI
18.08
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • Molecular Biology of the Cell (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
  • Takeda Science Foundation
  • Ministry of Education, Culture, Sports, Science and Technology
  • Kato Memorial Bioscience Foundation
  • University of California, San Diego
  • Japan Society for the Promotion of Science (23247034)
  • RIKEN
Topics
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords
Salmonella, autophagy, FIP200, Salmonella-containing vacuole, epithelial cells, host-pathogen interaction
MeSH terms
Autophagy-Related Proteins, Animals, Autophagy, Membrane Proteins, Microtubule-Associated Proteins, Phagosomes, Salmonella, Salmonella Infections, Vacuoles, Phosphatidylinositol 3-Kinases, Vesicular Transport Proteins, NIH 3T3 Cells, Intracellular Signaling Peptides and Proteins, Mice, Focal Adhesion Kinase 1

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