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  1. Article ; Online: In Brief: Mitophagy: mechanisms and role in human disease.

    Springer, Maya Z / Macleod, Kay F

    The Journal of pathology

    2016  Volume 240, Issue 3, Page(s) 253–255

    Abstract: Mitophagy is a selective form of macro-autophagy in which mitochondria are specifically targeted for autophagic degradation. Mitophagy plays an important role in cellular homeostasis by eliminating dysfunctional mitochondria and reducing mitochondrial ... ...

    Abstract Mitophagy is a selective form of macro-autophagy in which mitochondria are specifically targeted for autophagic degradation. Mitophagy plays an important role in cellular homeostasis by eliminating dysfunctional mitochondria and reducing mitochondrial mass as an adaptive response to stress. Cells execute mitophagy through several non-redundant mechanisms, including the PINK1/Parkin partnership, which modulates turnover of depolarized mitochondria, and stress-induced BNIP3, NIX, and FUNDC1 molecular adaptors, which interact directly with LC3 to promote mitophagy. These pathways are deregulated in human diseases, including cancer, neurodegeneration, metabolic disorders, muscle atrophy, ageing, and inflammation, reflecting the importance of mitophagy as a cellular housekeeping function. Copyright © 2016 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
    MeSH term(s) Adaptation, Physiological ; Aging/genetics ; Aging/physiology ; Autophagy ; Homeostasis ; Humans ; Inflammation/genetics ; Inflammation/physiopathology ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Metabolic Diseases/genetics ; Metabolic Diseases/physiopathology ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Mitochondria/pathology ; Mitochondria/physiology ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitophagy/physiology ; Models, Biological ; Muscular Atrophy/genetics ; Muscular Atrophy/physiopathology ; Neoplasms/genetics ; Neoplasms/physiopathology ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/physiopathology ; Protein Interaction Maps ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins/metabolism ; Signal Transduction ; Stress, Physiological ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
    Chemical Substances BNIP3 protein, human ; BNIP3L protein, human ; FUNDC1 protein, human ; MAP1LC3A protein, human ; Membrane Proteins ; Microtubule-Associated Proteins ; Mitochondrial Proteins ; Proto-Oncogene Proteins ; Tumor Suppressor Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; parkin protein (EC 2.3.2.27)
    Language English
    Publishing date 2016-09-29
    Publishing country England
    Document type Journal Article
    ZDB-ID 3119-7
    ISSN 1096-9896 ; 0022-3417
    ISSN (online) 1096-9896
    ISSN 0022-3417
    DOI 10.1002/path.4774
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.12: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: BNIP3-dependent mitophagy promotes cytosolic localization of LC3B and metabolic homeostasis in the liver.

    Springer, Maya Z / Poole, Logan P / Drake, Lauren E / Bock-Hughes, Althea / Boland, Michelle L / Smith, Alexandra G / Hart, John / Chourasia, Aparajita H / Liu, Ivan / Bozek, Grazyna / Macleod, Kay F

    Autophagy

    2021  Volume 17, Issue 11, Page(s) 3530–3546

    Abstract: Mitophagy formed the basis of the original description of autophagy by Christian de Duve when he demonstrated that GCG (glucagon) induced macroautophagic/autophagic turnover of mitochondria in the liver. However, the molecular basis of liver-specific ... ...

    Abstract Mitophagy formed the basis of the original description of autophagy by Christian de Duve when he demonstrated that GCG (glucagon) induced macroautophagic/autophagic turnover of mitochondria in the liver. However, the molecular basis of liver-specific activation of mitophagy by GCG, or its significance for metabolic stress responses in the liver is not understood. Here we show that BNIP3 is required for GCG-induced mitophagy in the liver through interaction with processed LC3B; an interaction that is also necessary to localize LC3B out of the nucleus to cytosolic mitophagosomes in response to nutrient deprivation. Loss of BNIP3-dependent mitophagy caused excess mitochondria to accumulate in the liver, disrupting metabolic zonation within the liver parenchyma, with expansion of zone 1 metabolism at the expense of zone 3 metabolism. These results identify BNIP3 as a regulator of metabolic homeostasis in the liver through its effect on mitophagy and mitochondrial mass distribution.
    MeSH term(s) Animals ; Cells, Cultured ; Cytosol/metabolism ; Glucagon/metabolism ; Glucagon/pharmacology ; Homeostasis ; Humans ; Liver/cytology ; Liver/drug effects ; Liver/metabolism ; Membrane Proteins/deficiency ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Mice, Knockout ; Mice, Transgenic ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Mitochondria, Liver/metabolism ; Mitochondrial Proteins/deficiency ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitophagy/drug effects ; Mitophagy/genetics ; Mitophagy/physiology ; Proto-Oncogene Proteins/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
    Chemical Substances BNIP3 protein, human ; BNip3 protein, mouse ; MAP1LC3B protein, human ; Map1lc3b protein, mouse ; Membrane Proteins ; Microtubule-Associated Proteins ; Mitochondrial Proteins ; Proto-Oncogene Proteins ; RNA, Messenger ; Glucagon (9007-92-5)
    Language English
    Publishing date 2021-02-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2021.1877469
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6741: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Expanding perspectives on the significance of mitophagy in cancer.

    Drake, Lauren E / Springer, Maya Z / Poole, Logan P / Kim, Casey J / Macleod, Kay F

    Seminars in cancer biology

    2017  Volume 47, Page(s) 110–124

    Abstract: Mitophagy is a selective mode of autophagy in which mitochondria are specifically targeted for degradation at the autophagolysosome. Mitophagy is activated by stresses such as hypoxia, nutrient deprivation, DNA damage, inflammation and mitochondrial ... ...

    Abstract Mitophagy is a selective mode of autophagy in which mitochondria are specifically targeted for degradation at the autophagolysosome. Mitophagy is activated by stresses such as hypoxia, nutrient deprivation, DNA damage, inflammation and mitochondrial membrane depolarization and plays a role in maintaining mitochondrial integrity and function. Defects in mitophagy lead to mitochondrial dysfunction that can affect metabolic reprogramming in response to stress, alter cell fate determination and differentiation, which in turn affects disease incidence and etiology, including cancer. Here, we discuss how different mitophagy adaptors and modulators, including Parkin, BNIP3, BNIP3L, p62/SQSTM1 and OPTN, are regulated in response to physiological stresses and deregulated in cancers. Additionally, we explore how these different mitophagy control pathways coordinate with each other. Finally, we review new developments in understanding how mitophagy affects stemness, cell fate determination, inflammation and DNA damage responses that are relevant to understanding the role of mitophagy in cancer.
    MeSH term(s) Adaptation, Biological ; Animals ; Autophagy ; DNA Damage ; Energy Metabolism ; Humans ; Inflammation/genetics ; Inflammation/metabolism ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitophagy ; Neoplasms/genetics ; Neoplasms/metabolism ; Signal Transduction ; Stress, Physiological
    Language English
    Publishing date 2017-04-24
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1033980-2
    ISSN 1096-3650 ; 1044-579X
    ISSN (online) 1096-3650
    ISSN 1044-579X
    DOI 10.1016/j.semcancer.2017.04.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2922: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Small molecules inhibit STAT3 activation, autophagy, and cancer cell anchorage-independent growth.

    Zhou, Donghui / Springer, Maya Z / Xu, David / Liu, Degang / Hudmon, Andy / Macleod, Kay F / Meroueh, Samy O

    Bioorganic & medicinal chemistry

    2017  Volume 25, Issue 12, Page(s) 2995–3005

    Abstract: Triple-negative breast cancers (TNBCs) lack the signature targets of other breast tumors, such as HER2, estrogen receptor, and progesterone receptor. These aggressive basal-like tumors are driven by a complex array of signaling pathways that are ... ...

    Abstract Triple-negative breast cancers (TNBCs) lack the signature targets of other breast tumors, such as HER2, estrogen receptor, and progesterone receptor. These aggressive basal-like tumors are driven by a complex array of signaling pathways that are activated by multiple driver mutations. Here we report the discovery of 6 (KIN-281), a small molecule that inhibits multiple kinases including maternal leucine zipper kinase (MELK) and the non-receptor tyrosine kinase bone marrow X-linked (BMX) with single-digit micromolar IC
    MeSH term(s) Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacology ; Autophagy/drug effects ; Breast/drug effects ; Breast/metabolism ; Breast/pathology ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Female ; Humans ; Molecular Docking Simulation ; Protein Kinase Inhibitors/chemistry ; Protein Kinase Inhibitors/pharmacology ; STAT3 Transcription Factor/antagonists & inhibitors ; STAT3 Transcription Factor/metabolism ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/pharmacology ; Triple Negative Breast Neoplasms/drug therapy ; Triple Negative Breast Neoplasms/metabolism ; Triple Negative Breast Neoplasms/pathology ; Tumor Suppressor Protein p53/metabolism
    Chemical Substances Antineoplastic Agents ; Protein Kinase Inhibitors ; STAT3 Transcription Factor ; Small Molecule Libraries ; Tumor Suppressor Protein p53
    Language English
    Publishing date 2017-03-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 1161284-8
    ISSN 1464-3391 ; 0968-0896
    ISSN (online) 1464-3391
    ISSN 0968-0896
    DOI 10.1016/j.bmc.2017.03.048
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3815: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Active and dynamic mitochondrial S-depalmitoylation revealed by targeted fluorescent probes.

    Kathayat, Rahul S / Cao, Yang / Elvira, Pablo D / Sandoz, Patrick A / Zaballa, María-Eugenia / Springer, Maya Z / Drake, Lauren E / Macleod, Kay F / van der Goot, F Gisou / Dickinson, Bryan C

    Nature communications

    2018  Volume 9, Issue 1, Page(s) 334

    Abstract: The reversible modification of cysteine residues by thioester formation with palmitate (S-palmitoylation) is an abundant lipid post-translational modification (PTM) in mammalian systems. S-palmitoylation has been observed on mitochondrial proteins, ... ...

    Abstract The reversible modification of cysteine residues by thioester formation with palmitate (S-palmitoylation) is an abundant lipid post-translational modification (PTM) in mammalian systems. S-palmitoylation has been observed on mitochondrial proteins, providing an intriguing potential connection between metabolic lipids and mitochondrial regulation. However, it is unknown whether and/or how mitochondrial S-palmitoylation is regulated. Here we report the development of mitoDPPs, targeted fluorescent probes that measure the activity levels of "erasers" of S-palmitoylation, acyl-protein thioesterases (APTs), within mitochondria of live cells. Using mitoDPPs, we discover active S-depalmitoylation in mitochondria, in part mediated by APT1, an S-depalmitoylase previously thought to reside in the cytosol and on the Golgi apparatus. We also find that perturbation of long-chain acyl-CoA cytoplasm and mitochondrial regulatory proteins, respectively, results in selective responses from cytosolic and mitochondrial S-depalmitoylases. Altogether, this work reveals that mitochondrial S-palmitoylation is actively regulated by "eraser" enzymes that respond to alterations in mitochondrial lipid homeostasis.
    MeSH term(s) A549 Cells ; Acyl Coenzyme A/metabolism ; Fluorescent Dyes/metabolism ; HEK293 Cells ; HeLa Cells ; Humans ; Kinetics ; Lipoylation ; MCF-7 Cells ; Microscopy, Confocal ; Mitochondria/metabolism ; Mitochondrial Dynamics ; RNA Interference ; Thiolester Hydrolases/genetics ; Thiolester Hydrolases/metabolism
    Chemical Substances Acyl Coenzyme A ; Fluorescent Dyes ; LYPLA1 protein, human (EC 3.1.2.-) ; Thiolester Hydrolases (EC 3.1.2.-)
    Language English
    Publishing date 2018-01-23
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-017-02655-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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