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Autophagy and p/SQSTM

Autophagy and p/SQSTM

Fluorescence observation was performed on glass-bottom dishes MatTek coated with 0. Autophagy and p/SQSTM, A. AHeLa cells were Autophagy and p/SQSTM Autophavy siRNA plus different Ahtophagy constructs and RFP-LC3. The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Due to marked accumulation of p62 and its phosphorylated forms in liver-specific autophagy-deficient mice e. Article MathSciNet CAS PubMed PubMed Central ADS Google Scholar Mastronarde, D. Cel Metab. Autophagy and p/SQSTM

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To determine the function of Atg5 in autophagosome formation to mycobacteria in DC, we examined the localization of LAMP1 or MHC II to ubiquitinated mycobacteria in JAWSII cells transfected with Atg5 siRNA Figure 7E, F.

Atg5 depletion decreased the proportion of LAMP1-positive or MHC II-positive ubiquitinated mycobacteria, suggesting that Atg5 functions in the fusion of lysosomes with mycobacterial autophagosomes in DC. The induction of autophagy can eliminate M. tuberculosis in phagocytic cells [ 37 , 38 ], but the precise mechanism by which mycobacterial infection induces autophagy in phagocytic cells is not fully understood.

Previous reports demonstrated that M. tuberculosis infection itself did not induce autophagy in infected macrophages [ 16 , 26 , 39 ].

However, other studies demonstrated that autophagosomes were formed in response to mycobacteria infection in macrophages [ 36 ]. Recently, it was demonstrated that M. tuberculosis infection induced autophagy but impaired the autophagic flux in human primary macrophages and DC [ 20 , 40 ].

In this study, we demonstrated that autophagosome markers localized to M. tuberculosis in BMDC but not in BMM Figure 1. In DC cell lines, we also showed that autophagosomes are formed in response to M.

tuberculosis infection Figure 2 , and found that lysosomal vesicles fuse with mycobacterial autophagosomes in DC Figure 4. Since autophagy is thought to be involved in antigen presentation via MHC II [ 22 ], it is assumed that autophagy promotes the presentation of mycobacterial antigens in DC.

tuberculosis infection induced selective autophagy in DC and that mycobacterial autophagosomes fuse with lysosomes followed by the recruitment of MHC II. What is the initial event that triggers the induction of autophagosome formation to mycobacteria in phagocytic cells? The ubiquitination of bacteria or bacterial phagosomes is important for selective autophagy because ubiquitinated substrates are associated with the autophagy adaptor proteins which recruit LC3 and autophagosome membranes [ 41 ].

In Mycobacterium marinum , the ubiquitination of this bacterium is dependent upon the ESAT-6 and ESX-1 secretion system [ 42 ]. ESAT-6 of M. marinum disrupts the phagosomal membranes to assist bacilli escape from phagosomes to the cytosol [ 43 - 46 ].

tuberculosis can also damage the phagosome membrane and translocate from phagosomes to the cytosol in a mechanism that is dependent upon the ESAT-6 and ESX-1 secretion system [ 47 , 48 ].

In macrophages, the permeabilization of the phagosomal membrane signals the ubiquitination of M. tuberculosis [ 36 , 49 , 50 ]. Our results suggest that the initial step for ubiquitination of mycobacteria in DC is also triggered by the permeabilization of phagosomal membrane by ESAT-6 because BCG bacilli were not ubiquitinated in DC data not shown.

Recently, an E3 ligase was identified that interacts with NDP52 and is responsible for ubiquitination of Salmonella [ 51 ]. Manzanillo et al.

demonstrated that a ubiquitin ligase, Parkin mediates the ubiquitination of intracellular bacteria in macrophages [ 50 ]. Results from the current study suggest the possibility that p62 mediates the recruitment of an E3 ligase for ubiquitination of M.

tuberculosis bacilli or bacilli-containing phagosomes in DC. Atg5 is involved in the elongation of isolation membrane in autophagosome formation [ 52 ]. We did not observe autophagosome membrane structures around infecting mycobacteria in DC by thin-section electron microscopy, however p62 and ubiquitin were recruited to mycobacteria in Atg5-knockdown DC Figures 6 and 7.

These results suggest that p62 and ubiquitin are recruited to infecting mycobacteria followed by the formation of autophagosome membrane depending on the function of Atg5. This hypothesis is consistent with the results that lysosomal markers do not localize to ubiqutinated mycobacteria in Atg5-knockdown DC Figure 7.

Atg16L is another autophagic-related protein involved in elongation of autophagic isolation membrane by forming an Atg5-AtgAtg16L complex [ 53 ]. We found that ubiquitin is recruited to M. tuberculosis but that LAMP1 does not localize to ubiquitinated mycobacteria in Atg16L-knockdown DC Figure S5.

These results suggest that ubiquitination of infected mycobacteria in DC is followed by formation of the autophagosome membrane and the autolysosome. We found that autophagosomal markers did not localize to infected mycobacteria in macrophages, but did so in DC Figure 1.

tuberculosis than those of macrophages. We have previously demonstrated that depletion of Coronin-1a leads the autophagosome formation to infecting M. tuberculosis in macrophages [ 26 ]. Coronin-1a associates with F-actin and localizes to mycobacterial phagosomes [ 54 , 55 ], suggesting that Coronin-1a supports the phagosomal membranes in macrophages but not in DC.

However, proteomic analysis revealed that Coronin-1a localizes to mycobacterial phagosomes in both macrophages and DC [ 56 ], suggesting that other proteins localizing to mycobacterial phagosomes in macrophages but not in DC would contribute the autophagosome formation to infecting mycobacteria.

In conclusion, M. tuberculosis infection in DC induced autophagosome formation followed by the fusion with lysosomes and MHC II recruitment. p62 and Atg5 function in the initiation and progression of autophagosome formation to M. tuberculosis , respectively. Thus, p62 mediates the ubiquitination of M.

tuberculosis and Atg5 is involved in the fusion of lysosomes with mycobacterial autophagosomes. These results imply that autophagosome formation in M.

Verification of co-localization between mycobacteria and autophagic proteins. i Split the image into channels. ii Make the binary image for each channel. iii Merge the binary images to verify the co-localization.

Quantification of band intensity for LC3-II. The quantification of band intensity for LC3-II in Figure 2E was shown. The proportion of LC3-positive A , ppositive B or ubiquitin-positive C M. Ubiqutination of mycobacteria in JAWSII cells. A Immunoblot analysis of JAWSII cells transfected with siRNA for autophagy-related genes.

JAWSII cells transfected with siRNA for p62 or Atg5 genes for 48 h were subjected to immunoblot analysis using the indicated antibodies. B The proportion of ubiquitinated mycobacteria in JAWSII cells. JAWSII cells transfected with siRNA for p62 or Atg5 were infected with DsRed-expressing M.

tuberculosis for 24 h and immunostained with anti-ubiquitin antibody. Ubiquitination of mycobacteria in Atg16L-knockdown DC. A Immunoblot analysis of DC2. B The proportion of ubiquitinated mycobacteria in Atg16L-knockdown DC. C The proportion of LAMP1 localization to ubiqutinated mycobacteria in Atg16L-knockdown DC.

tuberculosis and immunostained with anti-LAMP1 and anti-ubiquitin antibodies. We thank Dr. Toshi Nagata and Dr. Masato Uchijima Hamamatsu University School of Medicine, Hamamatsu, Japan for their helpful discussion. We also thank Ms. Keiko Sugaya and Ms.

Yumiko Suzuki Hamamatsu University School of Medicine for their excellent assistance. Conceived and designed the experiments: SS KT YK.

Performed the experiments: SS. Analyzed the data: SS KT. Wrote the manuscript: SS KT. Browse Subject Areas? Click through the PLOS taxonomy to find articles in your field. Article Authors Metrics Comments Media Coverage Reader Comments Figures.

Abstract Mycobacterium tuberculosis is an intracellular pathogen that can survive within phagocytic cells by inhibiting phagolysosome biogenesis. Materials and Methods Ethics statement Animal experiments in this study were approved by the Hamamatsu University School of Medicine Animal Care Committees at the Center Animal Care facility permit number: RNA interference siRNA duplexes were synthesized by Sigma-Aldrich St.

Fluorescence microscopy and immunoblotting analysis Immunofluorescence microscopic analysis was performed as previously described [ 3 ].

Infection with mycobacteria For observation by fluorescence microscopy, siRNA-transfected DC were scraped 48 h after transfection and grown on round coverslips in well plates for a further 12 h. Thin-section electron microscopy DC2.

Results Autophagosome formation to M. tuberculosis in DC To assess whether autophagosomes are formed around M. Download: PPT. Figure 1. Localization of autophagosome markers to M. tuberculosis in BMDC. Figure 2. Autophagy induction in response to infection of M. tuberculosis in DC cell lines.

Maturation of mycobacterial autophagosomes We examined the kinetics of localization of LC3, p62 or ubiquitin to M. Figure 3. Maturation of mycobacterial autophagosomes in DC2. MHC II localizes to mycobacterial autophagosomes Due to the fact that MHC II localizes to late endosomal and lysosomal compartments [ 33 ] and also localizes to autophagosomes [ 34 ], we next examined the localization of MHC II to mycobacterial autophagosomes in DC.

Figure 5. Localization of MHC class II to mycobacterial autophagosomes in DC. Ubiquitination of mycobacteria is pdependent To investigate the mechanism underlying autophagosome formation to M.

Atg5 functions in autolysosome biogenesis To further investigate the function of Atg5 in autophagosome formation to mycobacteria in DC, we observed the ultrastructures of M. Figure 7. Atg5-dependent localization of LAMP1 and MHC class II to mycobacterial autophagosomes.

Discussion The induction of autophagy can eliminate M. Supporting Information. Figure S1. s TIF. Figure S2. Figure S3. Figure S4. Figure S5. Acknowledgments We thank Dr. Author Contributions Conceived and designed the experiments: SS KT YK. References 1. Armstrong JA, Hart PD Response of cultured macrophages to Mycobacterium tuberculosis, with observations on fusion of lysosomes with phagosomes.

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Oncotarget a primarily oncology-focused, peer-reviewed, open access journal Nutritional guidelines to maximize p/QSTM impact Autophagy and p/SQSTM insightful Autophagy and p/SQSTM eliminate borders ahd specialties by linking different fields of oncology, cancer research and nad sciences; Autophagy and p/SQSTM foster application of basic and clinical science. Its scope is unique. The term "oncotarget" encompasses all molecules, pathways, cellular functions, cell types, and even tissues that can be viewed as targets relevant to cancer as well as other diseases. The term was introduced in the inaugural EditorialIntroducing Oncotarget. As of January 1,Oncotarget has shifted to a continuous publishing model. Autophsgy correspondence and Autophagy and p/SQSTM requests to Dr. John H. Brumell, Cell Biology Increase workout effectiveness, Hospital for Sick Children, University Avenue, Toronto, ON M5G 1X8, Canada. E-mail address: john. brumell sickkids. Yiyu T. ZhengShahab ShahnazariAndreas BrechTrond LamarkTerje JohansenJohn H.

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