We are analyzing https://link.springer.com/chapter/10.1007/978-3-642-00302-8_1.

Title:
An Overview of the Molecular Mechanism of Autophagy | SpringerLink
Description:
Autophagy is a highly conserved cellular degradation process in which portions of cytosol and organelles are sequestered into a double-membrane vesicle, an autophagosome, and delivered into a degradative organelle, the vacuole/lysosome, for breakdown and eventual...
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Keywords {🔍}

google, scholar, pubmed, cas, autophagy, cell, biol, klionsky, ohsumi, protein, mol, chem, atg, yeast, kinase, pathway, vacuole, mizushima, saccharomyces, cerevisiae, formation, yoshimori, noda, essential, selective, targeting, sci, required, autophagosome, autophagic, cytoplasm, structure, chapter, molecular, scott, stromhaug, kim, kominami, levine, mechanism, machinery, phosphatidylinositol, complex, transport, ueno, shintani, degradation, role, genes, reggiori,

Topics {✒️}

oligomeric α-mannosidase requires camp-dependent protein kinase cyclic amp-protein kinase cyclin-dependent kinase pho85p amp-activated protein kinase phosphatidylinositol 3-kinase/protein kinase pre-autophagosomal structure responsible pre-autophagosomal structure organized protein-activating enzyme essential month download article/chapter rapamycin-induced translational derepression huntingtin-induced cell death p150·ptdins 3-kinase complex human apg3p/aut1p homologue protein-conjugating enzyme essential ubp3p/bre5p ubiquitin protease vesicle-mediated protein transport apg12-apg5 conjugate pre-autophagosomal structure organization reversible modification regulates camp-protein kinase apg12-conjugating enzyme privacy choices/manage cookies membrane-binding state phosphatidylinositol 3-kinase complexes protein conjugation system atg1 kinase complex tissues activates mtor atg14p directs association drosophila fat body de winde jh signaling environmental conditions device instant download phosphatidylinositol kinase homologue eif2α kinase gcn2 phosphatidylinositol transfer protein houben-weerts jh vps15 protein kinase large oligomeric protein phosphoinositide-binding module cargo proteins facilitate atg16l complex specifies ccz1-mon1 complex atg11 links cargo ulk1-dependent cycling pre-autophagosomal structure kinome identifies ulk1 authentic e2 enzyme de novo formation autophagosomal membrane depending

Questions {❓}

Does vacuolar targeting of Cvt17/Aut5p affect its function?
Høyer-Hansen M, Jäättelä M (2007) AMP-activated protein kinase: a universal regulator of autophagy?
Levine B, Yuan J (2005) Autophagy in cell death: an innocent convict?

Schema {🗺️}

ScholarlyArticle:
      headline:An Overview of the Molecular Mechanism of Autophagy
      pageEnd:32
      pageStart:1
      image:https://media.springernature.com/w153/springer-static/cover/book/978-3-642-00302-8.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Autophagy in Infection and Immunity
         isbn:
            978-3-642-00302-8
            978-3-642-00301-1
         type:Book
      publisher:
         name:Springer Berlin Heidelberg
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Zhifen Yang
            affiliation:
                  name:University of Michigan
                  address:
                     name:Life Sciences Institute and Departments of Molecular, Cellular and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Daniel J. Klionsky
            affiliation:
                  name:University of Michigan
                  address:
                     name:Life Sciences Institute and Departments of Molecular, Cellular and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:Autophagosome Formation, Autophagic Activity, Selective Autophagy, Active Cysteine, Atg16 Complex
      description:Autophagy is a highly conserved cellular degradation process in which portions of cytosol and organelles are sequestered into a double-membrane vesicle, an autophagosome, and delivered into a degradative organelle, the vacuole/lysosome, for breakdown and eventual recycling of the resulting macromolecules. This process relieves the cell from various stress conditions. Autophagy plays a critical role during cellular development and differentiation, functions in tumor suppression, and may be linked to life span extension. Autophagy also has diverse roles in innate and adaptive immunity, such as resistance to pathogen invasion. Substantial progress has been made in the identification of many autophagy-related (ATG) genes that are essential to drive this cellular process, including both selective and nonselective types of autophagy. Identification of the ATG genes in yeast, and the finding of orthologs in other organisms, reveals the conservation of the autophagic machinery in all eukaryotes. Here, we summarize our current knowledge about the machinery and molecular mechanism of autophagy.
      datePublished:2009
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Book:
      name:Autophagy in Infection and Immunity
      isbn:
         978-3-642-00302-8
         978-3-642-00301-1
Organization:
      name:Springer Berlin Heidelberg
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Michigan
      address:
         name:Life Sciences Institute and Departments of Molecular, Cellular and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, USA
         type:PostalAddress
      name:University of Michigan
      address:
         name:Life Sciences Institute and Departments of Molecular, Cellular and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Zhifen Yang
      affiliation:
            name:University of Michigan
            address:
               name:Life Sciences Institute and Departments of Molecular, Cellular and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, USA
               type:PostalAddress
            type:Organization
      name:Daniel J. Klionsky
      affiliation:
            name:University of Michigan
            address:
               name:Life Sciences Institute and Departments of Molecular, Cellular and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Life Sciences Institute and Departments of Molecular, Cellular and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, USA
      name:Life Sciences Institute and Departments of Molecular, Cellular and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, USA
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