The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
The Adaptor Protein p62/SQSTM1 Targets Invading Bacteria to the Autophagy Pathway
Abstract
Autophagy, a cellular degradative pathway, plays a key role in protecting the cytosol from bacterial colonization, but the mechanisms of bacterial recognition by this pathway are unclear. Autophagy is also known to degrade cargo tagged by ubiquitinated proteins, including aggregates of misfolded proteins, and peroxisomes. Autophagy of ubiquitinated cargo requires p62 (also known as SQSTM1), an adaptor protein with multiple protein-protein interaction domains, including a ubiquitin-associated (UBA) domain for ubiquitinated cargo binding and an LC3 interaction region (LIR) for binding the autophagy protein LC3. Previous studies demonstrated that the intracellular bacterial pathogen Salmonella typhimurium is targeted by autophagy during infection of host cells. Here we show that p62 is recruited to S. typhimurium targeted by autophagy, and that the recruitment of p62 is associated with ubiquitinated proteins localized to the bacteria. Expression of p62 is required for efficient autophagy of bacteria, as well as restriction of their intracellular replication. Our studies demonstrate that the surveillance of misfolded proteins and bacteria occurs via a conserved pathway, and they reveal a novel function for p62 in innate immunity.
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Citations
Cites
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
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“Discussion In previous studies, p62 has been found in many cellular inclusions, including Mallory bodies in chronic liver disease (25), aggresome-like induced structures induced by puromycin treatment (13), Lewy bodies in Parkinson’s disease, and neurofibrillary tangles in Alzheimer’s disease (25, 26).”
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Self-citationThe role of autophagy during the early neonatal starvation period
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BackgroundStructural Basis for Sorting Mechanism of p62 in Selective Autophagy
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Self-citationAutophagy Recognizes Intracellular Salmonella enterica serovar Typhimurium in Damaged Vacuoles
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Cited by
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Self-citationGuidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
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Autophagy in infection, inflammation and immunity
Deretic, V., Saitoh, T., & Akira, S. (2013) · Nature Reviews Immunology · doi:10.1038/nri3532 · Cited by 1,919
Metadata
- Authors
- Zheng, Y. T., Shahnazari, S., Brech, A., Lamark, T., Johansen, T., & Brumell, J. H.
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-11-01
- Volume
- 183
- Issue
- 9
- Pages
- 5909-5916
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W2106195012
- Cited by
- 581
- References
- 9
- FWCI
- 28.79
- Type
- journal article
- Language
- en
- Open access
- closed
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- Zheng, Y. T., Shahnazari, S., Brech, A., Lamark, T., Johansen, T., & Brumell, J. H. (2009). The Adaptor Protein p62/SQSTM1 Targets Invading Bacteria to the Autophagy Pathway. The Journal of Immunology. https://doi.org/10.4049/jimmunol.0900441
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