Abstract
Macroautophagy (‘autophagy’), is the process by which cells can form a double-membraned vesicle that encapsulates material to be degraded by the lysosome. This can include complex structures such as damaged mitochondria, peroxisomes, protein aggregates and large swathes of cytoplasm that can not be processed efficiently by other means of degradation. Recycling of amino acids and lipids through autophagy allows the cell to form intracellular pools that aid survival during periods of stress, including growth factor deprivation, amino acid starvation or a depleted oxygen supply. One of the major functions of autophagy that has emerged over the last decade is its importance as a safeguard against infection. The ability of autophagy to selectively target intracellular pathogens for destruction is now regarded as a key aspect of the innate immune response. However, pathogens have evolved mechanisms to either evade or reconfigure the autophagy pathway for their own survival. Understanding how pathogens interact with and manipulate the host autophagy pathway will hopefully provide a basis for combating infection and increase our understanding of the role and regulation of autophagy. Herein, we will discuss how the host cell can identify and target invading pathogens and how pathogens have adapted in order to evade destruction by the host cell. In particular, we will focus on interactions between the mammalian autophagy gene 8 (ATG8) proteins and the host and pathogen effector proteins.
Highlights
Cells are alerted to intracellular pathogens by the presence of damaged membranes
The author declares that there are no competing interests associated with the manuscript
AIM, Atg8 interaction motif; ATG, autophagy gene; BCL-2, B-cell lymphoma 2; CMA, chaperone-mediated autophagy; EEA1, Early endosome antigen 1; FAK, Focal Adhesion Kinase; GABARAP, γ-aminobutyric acid receptor associated protein; GAS, Group A Streptococcus; GIM, GABARAP interaction motif; HOIL-1, Heme-oxidized IRP2 ubiquitin ligase 1; HOIP, HOIL-1-interacting protein; HP, hydrophobic pocket; LCV, Legionella-containing vacuole; LIM, LC3 interaction motif; LIR, LC3-interaction region; LLO, listeriolysin O; LUBAC, linear ubiquitin chain assembly complex; MAP1LC3 (LC3), Microtubule-associated proteins 1A/1B light chain 3B; MeV, Measles virus; mTOR, mechanistic target of rapamycin; M2, matrix 2; NBR1, next to BRCA1 gene 1; NDP52, nuclear dot protein 5; NF-κB, Nuclear factor -kappa-B; NRFB2, nuclear receptor binding factor; OPTN, optineurin; PAS, preautophagosomal structure; PE, phosphatidylethanolamine; PI3P, phosphatidylinositol-3-phosphate; PLEKHM1, pleckstrin homology domain containing family M member 1; SCV, Salmonella-containing vacuole; SNARE, Soluble NSF Attachment Protein Receptor; SQSTM1, sequestosome-1; STX17, Syntaxin17; TAX1BP1, Tax1-binding protein 1; TIAM1, T-cell lymphoma invasion and metastasis 1; TBC1D5, Tre-2/Bub2/Cdc16 1 domain family member 5; TBK1, TANK binding kinase 1; UBL, ubiquitin-like; UFIM, UFM1-interaction motif; UFM1, Ubiquitin-fold modifier 1; ULK1/2, unc-51-like kinase 1/2; WIPI, WD repeat domain phosphoinositide-interacting protein
Summary
Cells are alerted to intracellular pathogens by the presence of damaged membranes. This helps to recruit E3-ligases to generate the ‘eat-me’ signal.
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