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      Exophagy of annexin A2 via RAB11, RAB8A and RAB27A in IFN-γ-stimulated lung epithelial cells.

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          Abstract

          Annexin A2 (ANXA2), a phospholipid-binding protein, has multiple biological functions depending on its cellular localization. We previously demonstrated that IFN-γ-triggered ANXA2 secretion is associated with exosomal release. Here, we show that IFN-γ-induced autophagy is essential for the extracellular secretion of ANXA2 in lung epithelial cells. We observed colocalization of ANXA2-containing autophagosomes with multivesicular bodies (MVBs) after IFN-γ stimulation, followed by exosomal release. IFN-γ-induced exophagic release of ANXA2 could not be observed in ATG5-silenced or mutant RAB11-expressing cells. Furthermore, knockdown of RAB8A and RAB27A, but not RAB27B, reduced IFN-γ-triggered ANXA2 secretion. Surface translocation of ANXA2 enhanced efferocytosis by epithelial cells, and inhibition of different exophagic steps, including autophagosome formation, fusion of autophagosomes with MVBs, and fusion of amphisomes with plasma membrane, reduced ANXA2-mediated efferocytosis. Our data reveal a novel route of IFN-γ-induced exophagy of ANXA2.

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          Biogenesis and secretion of exosomes.

          Joanna Kowal, Mercedes Tkach, Clotilde Théry (2014)
          Although observed for several decades, the release of membrane-enclosed vesicles by cells into their surrounding environment has been the subject of increasing interest in the past few years, which led to the creation, in 2012, of a scientific society dedicated to the subject: the International Society for Extracellular Vesicles. Convincing evidence that vesicles allow exchange of complex information fuelled this rise in interest. But it has also become clear that different types of secreted vesicles co-exist, with different intracellular origins and modes of formation, and thus probably different compositions and functions. Exosomes are one sub-type of secreted vesicles. They form inside eukaryotic cells in multivesicular compartments, and are secreted when these compartments fuse with the plasma membrane. Interestingly, different families of molecules have been shown to allow intracellular formation of exosomes and their subsequent secretion, which suggests that even among exosomes different sub-types exist. Copyright © 2014 Elsevier Ltd. All rights reserved.
          Article 0 comments Cited 780 times – based on 0 reviews     Review now
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            A role for ubiquitin in selective autophagy.

            Vladimir Kirkin, David G McEwan, Ivana Novak … (2009)
            Ubiquitination is the hallmark of protein degradation by the 26S proteasome. However, the proteasome is limited in its capacity to degrade oligomeric and aggregated proteins. Removal of harmful protein aggregates is mediated by autophagy, a mechanism by which the cell sequesters cytosolic cargo and delivers it for degradation by the lysosome. Identification of autophagy receptors, such as p62/SQSTM1 and NBR1, which simultaneously bind both ubiquitin and autophagy-specific ubiquitin-like modifiers, LC3/GABARAP, has provided a molecular link between ubiquitination and autophagy. This review explores the hypothesis that ubiquitin represents a selective degradation signal suitable for targeting various types of cargo, ranging from protein aggregates to membrane-bound organelles and microbes.
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              Exosome: from internal vesicle of the multivesicular body to intercellular signaling device.

              K Denzer, M Kleijmeer, H Heijnen … (2000)
              Exosomes are small membrane vesicles that are secreted by a multitude of cell types as a consequence of fusion of multivesicular late endosomes/lysosomes with the plasma membrane. Depending on their origin, exosomes can play roles in different physiological processes. Maturing reticulocytes externalize obsolete membrane proteins such as the transferrin receptor by means of exosomes, whereas activated platelets release exosomes whose function is not yet known. Exosomes are also secreted by cytotoxic T cells, and these might ensure specific and efficient targeting of cytolytic substances to target cells. Antigen presenting cells, such as B lymphocytes and dendritic cells, secrete MHC class-I- and class-II-carrying exosomes that stimulate T cell proliferation in vitro. In addition, dendritic-cell-derived exosomes, when used as a cell-free vaccine, can eradicate established murine tumors. Although the precise physiological target(s) and functions of exosomes remain largely to be resolved, follicular dendritic cells (accessory cells in the germinal centers of secondary lymphoid organs) have recently been shown to bind B-lymphocyte-derived exosomes at their cell surface, which supports the notion that exosomes play an immunoregulatory role. Finally, since exosomes are derived from multivesicular bodies, their molecular composition might provide clues to the mechanism of protein and lipid sorting in endosomes.
              Article 0 comments Cited 269 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (iso-abbrev): Sci Rep
                Title: Scientific reports
                Publisher: Springer Science and Business Media LLC
                ISSN (Electronic): 2045-2322
                ISSN (Print): 2045-2322
                Publication date (Electronic): July 18 2017
                Volume: 7
                Issue: 1
                Affiliations
                [1 ] Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
                [2 ] Department of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
                [3 ] Center of Infectious Disease and Signaling Research, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
                [4 ] Department of Microbiology and Immunology, College of Medicine, Taipei Medical University, Taipei, Taiwan.
                [5 ] Department of Medical Laboratory Science and Biotechnology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
                [6 ] Departments of Microbiology & Immunology and Pediatrics, and Canadian Center for Vaccinology, Dalhousie University, Halifax, Canada.
                [7 ] Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan. cpchang@mail.ncku.edu.tw.
                [8 ] Department of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan. cpchang@mail.ncku.edu.tw.
                [9 ] Center of Infectious Disease and Signaling Research, College of Medicine, National Cheng Kung University, Tainan, Taiwan. cpchang@mail.ncku.edu.tw.
                [10 ] Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan, Taiwan. yslin1@mail.ncku.edu.tw.
                [11 ] Department of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan. yslin1@mail.ncku.edu.tw.
                [12 ] Center of Infectious Disease and Signaling Research, College of Medicine, National Cheng Kung University, Tainan, Taiwan. yslin1@mail.ncku.edu.tw.
                Article
                Publisher Item ID: 10.1038/s41598-017-06076-4
                DOI: 10.1038/s41598-017-06076-4
                PMC ID: 5516008
                PubMed ID: 28720835
                SO-VID: e5bbadc0-92c6-45c4-9286-7725de209294
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