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      Unconventional secretion of annexins and galectins

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          Abstract

          Eukaryotic cells have a highly evolved system of protein secretion, and dysfunction in this pathway is associated with many diseases including cancer, infection, metabolic disease and neurological disorders. Most proteins are secreted using the conventional endoplasmic reticulum (ER)/Golgi network and as such, this pathway is well-characterised. However, several cytosolic proteins have now been documented as secreted by unconventional transport pathways. This review focuses on two of these proteins families: annexins and galectins. The extracellular functions of these proteins are well documented, as are associations of their perturbed secretion with several diseases. However, the mechanisms and regulation of their secretion remain poorly characterised, and are discussed in this review.

          This review is part of a Special Issues of SCDB on ‘unconventional protein secretion’ edited by Walter Nickel and Catherine Rabouille .

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          The mechanisms of vesicle budding and fusion.

          Juan Bonifacino, Benjamin Glick (2004)
          Genetic and biochemical analyses of the secretory pathway have produced a detailed picture of the molecular mechanisms involved in selective cargo transport between organelles. This transport occurs by means of vesicular intermediates that bud from a donor compartment and fuse with an acceptor compartment. Vesicle budding and cargo selection are mediated by protein coats, while vesicle targeting and fusion depend on a machinery that includes the SNARE proteins. Precise regulation of these two aspects of vesicular transport ensures efficient cargo transfer while preserving organelle identity.
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            Active caspase-1 is a regulator of unconventional protein secretion.

            Martin F. Keller, Andreas Rüegg, Sabine Werner … (2008)
            Mammalian cells export most proteins by the endoplasmic reticulum/Golgi-dependent pathway. However, some proteins are secreted via unconventional, poorly understood mechanisms. The latter include the proinflammatory cytokines interleukin(IL)-1beta, IL-18, and IL-33, which require activation by caspase-1 for biological activity. Caspase-1 itself is activated by innate immune complexes, the inflammasomes. Here we show that secretion of the leaderless proteins proIL-1alpha, caspase-1, and fibroblast growth factor (FGF)-2 depends on caspase-1 activity. Although proIL-1alpha and FGF-2 are not substrates of the protease, we demonstrated their physical interaction. Secretome analysis using iTRAQ proteomics revealed caspase-1-mediated secretion of other leaderless proteins with known or unknown extracellular functions. Strikingly, many of these proteins are involved in inflammation, cytoprotection, or tissue repair. These results provide evidence for an important role of caspase-1 in unconventional protein secretion. By this mechanism, stress-induced activation of caspase-1 directly links inflammation to cytoprotection, cell survival, and regenerative processes.
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              Galectins: structure, function and therapeutic potential.

              Ri-Yao Yang, Gabriel Rabinovich, Fu-Tong Liu (2008)
              Galectins are a family of animal lectins that bind beta-galactosides. Outside the cell, galectins bind to cell-surface and extracellular matrix glycans and thereby affect a variety of cellular processes. However, galectins are also detectable in the cytosol and nucleus, and may influence cellular functions such as intracellular signalling pathways through protein-protein interactions with other cytoplasmic and nuclear proteins. Current research indicates that galectins play important roles in diverse physiological and pathological processes, including immune and inflammatory responses, tumour development and progression, neural degeneration, atherosclerosis, diabetes, and wound repair. Some of these have been discovered or confirmed by using genetically engineered mice deficient in a particular galectin. Thus, galectins may be a therapeutic target or employed as therapeutic agents for inflammatory diseases, cancers and several other diseases.
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                Author and article information

                Contributors
                Kevin Moreau
                Journal
                Journal ID (nlm-ta): Semin Cell Dev Biol
                Journal ID (iso-abbrev): Semin. Cell Dev. Biol
                Title: Seminars in Cell & Developmental Biology
                Publisher: Academic Press
                ISSN (Print): 1084-9521
                ISSN (Electronic): 1096-3634
                Publication date PMC-release: 1 November 2018
                Publication date (Print): November 2018
                Volume: 83
                Pages: 42-50
                Affiliations
                [0005]University of Cambridge, Metabolic Research Laboratories, Wellcome Trust-Medical Research Council Institute of Metabolic Science, Cambridge, CB2 0QQ, UK
                Author notes
                [* ]Corresponding author. km510@ 123456cam.ac.uk
                Article
                Publisher ID: S1084-9521(17)30582-7
                DOI: 10.1016/j.semcdb.2018.02.022
                PMC ID: 6565930
                PubMed ID: 29501720
                SO-VID: 8481d64b-fce2-49be-91a6-b740a53a1717
                Copyright © © 2018 The Authors
                License:

                This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 6 December 2017
                Date revision received : 23 February 2018
                Date accepted : 26 February 2018
                Categories
                Subject: Article

                ScienceOpen disciplines: Developmental biology
                Keywords: unconventional secretion,galectins,annexins,transport
                Data availability:
                ScienceOpen disciplines: Developmental biology
                Keywords: unconventional secretion, galectins, annexins, transport

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