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  • 1
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    Autophagy as a regulated pathway of cellular degradation (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-02
    Description: Macroautophagy is a dynamic process involving the rearrangement of subcellular membranes to sequester cytoplasm and organelles for delivery to the lysosome or vacuole where the sequestered cargo is degraded and recycled. This process takes place in all eukaryotic cells. It is highly regulated through the action of various kinases, phosphatases, and guanosine triphosphatases (GTPases). The core protein machinery that is necessary to drive formation and consumption of intermediates in the macroautophagy pathway includes a ubiquitin-like protein conjugation system and a protein complex that directs membrane docking and fusion at the lysosome or vacuole. Macroautophagy plays an important role in developmental processes, human disease, and cellular response to nutrient deprivation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2732363/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2732363/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klionsky, D J -- Emr, S D -- CA58689/CA/NCI NIH HHS/ -- GM53396/GM/NIGMS NIH HHS/ -- R01 GM053396/GM/NIGMS NIH HHS/ -- R01 GM053396-11/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 1;290(5497):1717-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Michigan, 830 North University, Ann Arbor, MI 48109-1048, USA. klionsky@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11099404" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Autophagy ; Cytoplasm/*metabolism ; Humans ; Lysosomes/metabolism/ultrastructure ; Membrane Fusion ; Organelles/*metabolism/ultrastructure ; Phagosomes/*metabolism/ultrastructure ; Proteins/metabolism ; Yeasts/genetics/metabolism/ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Autophagy fights disease through cellular self-digestion (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-02-29
    Description: Autophagy, or cellular self-digestion, is a cellular pathway involved in protein and organelle degradation, with an astonishing number of connections to human disease and physiology. For example, autophagic dysfunction is associated with cancer, neurodegeneration, microbial infection and ageing. Paradoxically, although autophagy is primarily a protective process for the cell, it can also play a role in cell death. Understanding autophagy may ultimately allow scientists and clinicians to harness this process for the purpose of improving human health.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2670399/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2670399/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mizushima, Noboru -- Levine, Beth -- Cuervo, Ana Maria -- Klionsky, Daniel J -- R01 AG021904/AG/NIA NIH HHS/ -- R01 AG021904-06/AG/NIA NIH HHS/ -- R03 AG019834/AG/NIA NIH HHS/ -- R03 AG019834-02/AG/NIA NIH HHS/ -- R21 AG025355/AG/NIA NIH HHS/ -- R21 AG025355-02/AG/NIA NIH HHS/ -- England -- Nature. 2008 Feb 28;451(7182):1069-75. doi: 10.1038/nature06639.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Cell Biology, Tokyo Medical and Dental University, Tokyo 113-8519, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18305538" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/physiology ; Animals ; Autophagy/immunology/*physiology ; Cell Death ; Cell Survival ; Humans ; Immunity, Innate/immunology ; Neoplasms/pathology ; Neurodegenerative Diseases/pathology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Autophagy in health and disease: a double-edged sword (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-06
    Description: Autophagy, the process by which cells recycle cytoplasm and dispose of excess or defective organelles, has entered the research spotlight largely owing to the discovery of the protein components that drive this process. Identifying the autophagy genes in yeast and finding orthologs in other organisms reveals the conservation of the mechanism of autophagy in eukaryotes and allows the use of molecular genetics and biology in different model systems to study this process. By mostly morphological studies, autophagy has been linked to disease processes. Whether autophagy protects from or causes disease is unclear. Here, we summarize current knowledge about the role of autophagy in disease and health.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1705980/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1705980/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shintani, Takahiro -- Klionsky, Daniel J -- GM53396/GM/NIGMS NIH HHS/ -- R01 GM053396/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Nov 5;306(5698):990-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Michigan, Life Sciences Institute, Ann Arbor, MI 48109-2216, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15528435" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Autophagy/*physiology ; Humans ; Infection/physiopathology ; Muscular Diseases/physiopathology ; Neoplasms/physiopathology ; Neurodegenerative Diseases/physiopathology ; Phagosomes/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    The histone H4 lysine 16 acetyltransferase hMOF regulates the outcome of autophagy (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-07-19
    Description: Autophagy is an evolutionarily conserved catabolic process involved in several physiological and pathological processes. Although primarily cytoprotective, autophagy can also contribute to cell death; it is thus important to understand what distinguishes the life or death decision in autophagic cells. Here we report that induction of autophagy is coupled to reduction of histone H4 lysine 16 acetylation (H4K16ac) through downregulation of the histone acetyltransferase hMOF (also called KAT8 or MYST1), and demonstrate that this histone modification regulates the outcome of autophagy. At a genome-wide level, we find that H4K16 deacetylation is associated predominantly with the downregulation of autophagy-related genes. Antagonizing H4K16ac downregulation upon autophagy induction results in the promotion of cell death. Our findings establish that alteration in a specific histone post-translational modification during autophagy affects the transcriptional regulation of autophagy-related genes and initiates a regulatory feedback loop, which serves as a key determinant of survival versus death responses upon autophagy induction.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4006103/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4006103/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fullgrabe, Jens -- Lynch-Day, Melinda A -- Heldring, Nina -- Li, Wenbo -- Struijk, Robert B -- Ma, Qi -- Hermanson, Ola -- Rosenfeld, Michael G -- Klionsky, Daniel J -- Joseph, Bertrand -- GM53396/GM/NIGMS NIH HHS/ -- R01 GM053396/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2013 Aug 22;500(7463):468-71. doi: 10.1038/nature12313. Epub 2013 Jul 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology Pathology, Cancer Centrum Karolinska, Karolinska Institutet, Stockholm 17176, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23863932" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation/drug effects ; *Autophagy/drug effects/genetics ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Down-Regulation/drug effects ; Epistasis, Genetic/drug effects ; Feedback, Physiological ; Histone Acetyltransferases/*metabolism ; Histones/*metabolism ; Humans ; Lysine/chemistry/metabolism ; Sirolimus/pharmacology ; Transcription, Genetic/drug effects/genetics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
    Electronic Resource
    Electronic Resource
    Vacuolar H+-ATPase: From mammals to yeast and back (1996)
    Springer
    Cellular and molecular life sciences 52 (1996), S. 1101-1110 
    Details
    ISSN: 1420-9071
    Keywords: Vacuolar H+-ATPase ; biogenesis ; assembly ; proton pump ; bovine ; yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Vacuolar H+-adenosine triphosphatase (V-ATPase) is composed of distinct catalytic (V1) and membrane (V0) sectors containing several subunits. The biochemistry of the enzyme was mainly studied in organelles from mammalian cells such as chromaffin granules and clathrin-coated vesicles. Subsequently, mammalian cDNAs and yeast genes encoding subunits of V-ATPase were cloned and sequenced. The sequence information revealed the relation between V- and F-ATPases that evolved from a common ancestor. The isolation of yeast genes encoding subunits of V-ATPase opened an avenue for molecular biology studies of the enzyme. Because V-ATPase is present in every known eukaryotic cell and provides energy for vital transport systems, it was anticipated that disruption of genes encoding V-ATPase subunits would be lethal. Fortunately, yeast cells can survive the absence of V-ATPase by ‘drinking’ the acidic medium. So far only yeast cells have been shown to be viable without an active V-ATPase. In contrast to yeast, mammalian cells may have more than one gene encoding each of the subunits of the enzyme. Some of these genes encode tissue- and/or organelle-specific subunits. Expression of these specific cDNAs in yeast cells may reveal their unique functions in mammalian cells. Following the route from mammals to yeast and back may prove useful in the study of many other complicated processes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01952108
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    Paper (German National Licenses)
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  • 6
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    Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole. (1996)
    National Academy of Sciences
    Details
    Publication Date: 1996-10-29
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 7
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    Ume6 transcription factor is part of a signaling cascade that regulates autophagy (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-06-25
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 8
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    Atg29 phosphorylation regulates coordination of the Atg17-Atg31-Atg29 complex with the Atg11 scaffold during autophagy initiation (2013)
    National Academy of Sciences
    Details
    Publication Date: 2013-07-15
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 9
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    Ume6 transcriptional control of ATG8 [Cell Biology] (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-07-11
    Description: Autophagy has been implicated in a number of physiological processes important for human heath and disease. Autophagy involves the formation of a double-membrane cytosolic vesicle, an autophagosome. Central to the formation of the autophagosome is the ubiquitin-like protein autophagy-related (Atg)8 (microtubule-associated protein 1 light chain 3/LC3 in mammalian cells). Following autophagy induction, Atg8 shows the greatest change in expression of any of the proteins required for autophagy. The magnitude of autophagy is, in part, controlled by the amount of Atg8; thus, controlling Atg8 protein levels is one potential mechanism for modulating autophagy activity. We have identified a negative regulator of ATG8 transcription, Ume6, which acts along with a histone deacetylase complex including Sin3 and Rpd3 to regulate Atg8 levels; deletion of any of these components leads to an increase in Atg8 and a concomitant increase in autophagic activity. A similar regulatory mechanism is present in mammalian cells, indicating that this process is highly conserved.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    Vacuolar H+-ATPase: From mammals to yeast and back (1996)
    Springer
    Details
    Publication Date: 1996-12-01
    Print ISSN: 0014-4754
    Topics: Biology , Medicine
    Published by Springer
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