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      Apocrine Secretion in Drosophila Salivary Glands: Subcellular Origin, Dynamics, and Identification of Secretory Proteins

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          Abstract

          In contrast to the well defined mechanism of merocrine exocytosis, the mechanism of apocrine secretion, which was first described over 180 years ago, remains relatively uncharacterized. We identified apocrine secretory activity in the late prepupal salivary glands of Drosophila melanogaster just prior to the execution of programmed cell death (PCD). The excellent genetic tools available in Drosophila provide an opportunity to dissect for the first time the molecular and mechanistic aspects of this process. A prerequisite for such an analysis is to have pivotal immunohistochemical, ultrastructural, biochemical and proteomic data that fully characterize the process. Here we present data showing that the Drosophila salivary glands release all kinds of cellular proteins by an apocrine mechanism including cytoskeletal, cytosolic, mitochondrial, nuclear and nucleolar components. Surprisingly, the apocrine release of these proteins displays a temporal pattern with the sequential release of some proteins ( e.g. transcription factor BR-C, tumor suppressor p127, cytoskeletal β-tubulin, non-muscle myosin) earlier than others ( e.g. filamentous actin, nuclear lamin, mitochondrial pyruvate dehydrogenase). Although the apocrine release of proteins takes place just prior to the execution of an apoptotic program, the nuclear DNA is never released. Western blotting indicates that the secreted proteins remain undegraded in the lumen. Following apocrine secretion, the salivary gland cells remain quite vital, as they retain highly active transcriptional and protein synthetic activity.

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          Most cited references103

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          Using FlyAtlas to identify better Drosophila melanogaster models of human disease.

          FlyAtlas, a new online resource, provides the most comprehensive view yet of expression in multiple tissues of Drosophila melanogaster. Meta-analysis of the data shows that a significant fraction of the genome is expressed with great tissue specificity in the adult, demonstrating the need for the functional genomic community to embrace a wide range of functional phenotypes. Well-known developmental genes are often reused in surprising tissues in the adult, suggesting new functions. The homologs of many human genetic disease loci show selective expression in the Drosophila tissues analogous to the affected human tissues, providing a useful filter for potential candidate genes. Additionally, the contributions of each tissue to the whole-fly array signal can be calculated, demonstrating the limitations of whole-organism approaches to functional genomics and allowing modeling of a simple tissue fractionation procedure that should improve detection of weak or tissue-specific signals.
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            Membrane fusion: grappling with SNARE and SM proteins.

            The two universally required components of the intracellular membrane fusion machinery, SNARE and SM (Sec1/Munc18-like) proteins, play complementary roles in fusion. Vesicular and target membrane-localized SNARE proteins zipper up into an alpha-helical bundle that pulls the two membranes tightly together to exert the force required for fusion. SM proteins, shaped like clasps, bind to trans-SNARE complexes to direct their fusogenic action. Individual fusion reactions are executed by distinct combinations of SNARE and SM proteins to ensure specificity, and are controlled by regulators that embed the SM-SNARE fusion machinery into a physiological context. This regulation is spectacularly apparent in the exquisite speed and precision of synaptic exocytosis, where synaptotagmin (the calcium-ion sensor for fusion) cooperates with complexin (the clamp activator) to control the precisely timed release of neurotransmitters that initiates synaptic transmission and underlies brain function.
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              The 26S proteasome: a molecular machine designed for controlled proteolysis.

              In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteasome pathway. The 26S proteasome is a 2.5-MDa molecular machine built from approximately 31 different subunits, which catalyzes protein degradation. It contains a barrel-shaped proteolytic core complex (the 20S proteasome), capped at one or both ends by 19S regulatory complexes, which recognize ubiquitinated proteins. The regulatory complexes are also implicated in unfolding and translocation of ubiquitinated targets into the interior of the 20S complex, where they are degraded to oligopeptides. Structure, assembly and enzymatic mechanism of the 20S complex have been elucidated, but the functional organization of the 19S complex is less well understood. Most subunits of the 19S complex have been identified, however, specific functions have been assigned to only a few. A low-resolution structure of the 26S proteasome has been obtained by electron microscopy, but the precise arrangement of subunits in the 19S complex is unclear.
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                Author and article information

                Contributors
                Role: Editor
                Journal
                PLoS One
                PLoS ONE
                plos
                plosone
                PLoS ONE
                Public Library of Science (San Francisco, USA )
                1932-6203
                2014
                14 April 2014
                : 9
                : 4
                : e94383
                Affiliations
                [1 ]Laboratory of Developmental Genetics, Institute of Experimental Endocrinology, Slovak Academy of Sciences, Bratislava, Slovakia,
                [2 ]Department of Genetics, Comenius University, Bratislava, Slovakia
                [3 ]Department of Anatomy and Cell Biology, Lorand Eötvös University, Budapest, Hungary
                [4 ]Institute of Molecular Pathology, Faculty of Military Health Sciences, University of Defence, Hradec Králové, Czech Republic
                [5 ]1st Department of Internal Medicine - Cardioangiology, Faculty of Medicine in Hradec Králové, Charles University in Prague, Hradec Králové, Czech Republic
                [6 ]Institute of Cellular Biology and Pathology, 1st Faculty of Medicine, Charles University in Prague, Prague, Czech Republic
                [7 ]Deutsches Krebsforschungszentrum, Heidelberg, Germany
                Technische Universität Dresden, Germany
                Author notes

                Competing Interests: The authors have declared that no competing interests exist.

                Conceived and designed the experiments: RF. Performed the experiments: RF ZD LM DBL MB PL MS PR HR LK JS OR. Analyzed the data: RF BMM IR PL MS DBL. Wrote the paper: RF.

                Article
                PONE-D-13-51389
                10.1371/journal.pone.0094383
                3986406
                24732043
                1900a649-6949-41d7-b7e8-526458c3fd31
                Copyright @ 2014

                This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

                History
                : 6 December 2013
                : 14 March 2014
                Page count
                Pages: 23
                Funding
                GACR (Grant Agency of Czech Republic) grant P302/11/1640 to B.M.M. ( www.gacr.cz); GACR grant P302/12/G157 to I.R. ( www.gacr.cz); University Centre of Excellence UNCE 204022 and Prvouk/LF1/1 from Charles University to I.R. ( www.cuni.cz); PMFHK Plan no. 1011 to P.R. ( www.pmfhk.cz); CZ.1.07/2.3.00/30.0022 to P.R. ( http://ec.europa.eu/esf/); VEGA (Scientific Grant Agency of the Slovak Academy of Sciences) 2/0170/10 to R.F. ( www.sav.sk); VEGA (Scientific Grant Agency of the Slovak Academy of Sciences) 2/0109/13 to R.F. ( www.sav.sk); MVTS-32060600/EC-INSTRUCT-FP7-211252 (Supporting Program for International Science and Technology Cooperation of the Slovak Academy of Sciences with 7th Framework Programme of the European Commission) grant to R.F.( http://cordis.europa.eu/fp7/home_en.html/ www.sav.sk); and EEA-Norwegian FM SK-0086 (European Economic Area and Norwegian Financial Mechanism) grant to R.F. ( http://eeagrants.org). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
                Categories
                Research Article
                Biology and Life Sciences
                Biochemistry
                Proteins
                Proteomes
                Cytochemistry
                Cell Biology
                Cell Processes
                Cell Death
                Signal Transduction
                Cell Signaling
                Cellular Structures and Organelles
                Molecular Cell Biology
                Developmental Biology
                Metamorphosis
                Organism Development
                Genetics
                Gene Function
                Organisms
                Animals
                Invertebrates
                Arthropoda
                Insects
                Drosophila
                Drosophila Melanogaster
                Research and Analysis Methods
                Model Organisms
                Animal Models

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                Uncategorized

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