We are analyzing https://link.springer.com/article/10.1007/s00018-015-2087-8.

Title:
Mitophagy programs: mechanisms and physiological implications of mitochondrial targeting by autophagy | Cellular and Molecular Life Sciences
Description:
Mitochondria are an essential source of ATP for cellular function, but when damaged, mitochondria generate a plethora of stress signals, which lead to cellular dysfunction and eventually programmed cell death. Thus, a major component of maintaining cellular homeostasis is the recognition and removal of dysfunctional mitochondria through autophagy-mediated degradation, i.e., mitophagy. Mitophagy further constitutes a developmental program, and undergoes a high degree of crosstalk with apoptosis. Reduced mitochondrial quality control is linked to disease pathogenesis, suggesting the importance of process elucidation as a clinical target. Recent work has revealed multiple mitophagy programs that operate independently or undergo crosstalk, and require modulated autophagy receptor activities at outer membranes of mitochondria. Here, we review these mitophagy programs, focusing on pathway mechanisms which recognize and target mitochondria for sequestration by autophagosomes, as well as mechanisms controlling pathway activities. Furthermore, we provide an introduction to the currently available methods for detecting mitophagy.
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Keywords {🔍}

pubmed, mitophagy, article, google, scholar, cas, mitochondrial, mitochondria, cell, central, autophagy, parkin, bnip, protein, lir, proteins, nix, biol, expression, fig, receptor, phosphorylation, receptors, atg, omm, cancer, activity, apoptosis, cells, death, membrane, degradation, autophagosomes, fusion, autophagosome, function, binding, response, mol, wang, chen, signaling, regulation, fundc, serine, conditions, addition, pink, increased, lcb,

Topics {✒️}

hsa-mir-125a-5p target nix parkin-ubiquitin-p62-mediated mitochondrial priming n-terminal α-helices anne hamacher-brady article hamacher-brady regulating parkin/pink1-dependent mitophagy mit/tfe transcription factors nathan ryan brady hsa-mir-125a-5p autophagy-inflammation-cell death axis mitochondria-targeted rfp–gfp fusion crispr/cas9 genome editing bax/bak-mediated entering pro-survival bcl-xl drp1-binding protein fis1 n-terminal sequence alignments multi-tiered homeostatic feedback high-resolution imaging difficult anti-apoptotic signaling antagonizes article download pdf gfp-lc3-g120a mutant unique c-terminal extension gamma-aminobutyric acid receptor canonical macroautophagy-mediated modes bax/bak-dependent release pro-survival bcl-2 members identical n-terminal lirs pro-survival bcl-2 proteins receptor-ligand interaction occurs tandem fluorescent-tagged lc3 stk3/stk4-mediated phosphorylation anti-apoptotic bcl-2 proteins remove parkin-ligated ubiquitin e3 ligase-mediated ubiquitylation antagonizes parkin-mediated mitophagy regulates pro-apoptotic bnip3 activate hif1α-mediated glycolysis mouse cytomegalovirus-induced proliferation atg8 family-interacting motif atg8-family-interacting motif increase parkin-mediated mitophagy parkin-mediated mitophagy utilize exert pro-autophagic activity hippo kinases stk3/stk4 bnip3-mediated apoptotic signaling autophagic machinery coordinates bnip3-mediated mitophagy participates rab gtpase-activating proteins pro-apoptotic bcl-2 subfamily pro-death apoptosis signaling

Schema {🗺️}

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         Mitophagy
         Nix
         Parkin E3 ligase
         Ubiquitin
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
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               type:PostalAddress
            type:Organization
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            address:
               name:Bioquant, University of Heidelberg, Heidelberg, Germany
               type:PostalAddress
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      affiliation:
            name:German Cancer Research Center (DKFZ)
            address:
               name:Systems Biology of Cell Death Mechanisms, German Cancer Research Center (DKFZ), Heidelberg, Germany
               type:PostalAddress
            type:Organization
            name:Heidelberg University Hospital
            address:
               name:Department of Surgery, Heidelberg University Hospital, Heidelberg, Germany
               type:PostalAddress
            type:Organization
            name:University of Heidelberg
            address:
               name:Bioquant, University of Heidelberg, Heidelberg, Germany
               type:PostalAddress
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      name:Lysosomal Systems Biology, German Cancer Research Center (DKFZ), Heidelberg, Germany
      name:Bioquant, University of Heidelberg, Heidelberg, Germany
      name:Systems Biology of Cell Death Mechanisms, German Cancer Research Center (DKFZ), Heidelberg, Germany
      name:Department of Surgery, Heidelberg University Hospital, Heidelberg, Germany
      name:Bioquant, University of Heidelberg, Heidelberg, Germany

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