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  1. Article ; Online: Protein palmitoylation and cancer.

    Ko, Pin-Joe / Dixon, Scott J

    EMBO reports

    2018  Volume 19, Issue 10

    Abstract: Protein S-palmitoylation is a reversible post-translational modification that alters the localization, stability, and function of hundreds of proteins in the cell. S-palmitoylation is essential for the function of both oncogenes (e.g., NRAS and EGFR) and ...

    Abstract Protein S-palmitoylation is a reversible post-translational modification that alters the localization, stability, and function of hundreds of proteins in the cell. S-palmitoylation is essential for the function of both oncogenes (e.g., NRAS and EGFR) and tumor suppressors (e.g., SCRIB, melanocortin 1 receptor). In mammalian cells, the thioesterification of palmitate to internal cysteine residues is catalyzed by 23 Asp-His-His-Cys (DHHC)-family palmitoyl S-acyltransferases while the removal of palmitate is catalyzed by serine hydrolases, including acyl-protein thioesterases (APTs). These enzymes modulate the function of important oncogenes and tumor suppressors and often display altered expression patterns in cancer. Targeting S-palmitoylation or the enzymes responsible for palmitoylation dynamics may therefore represent a candidate therapeutic strategy for certain cancers.
    MeSH term(s) Acyltransferases/genetics ; Humans ; Lipoylation/genetics ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Neoplasms/genetics ; Neoplasms/metabolism ; Protein Processing, Post-Translational/genetics ; Proteolysis ; Substrate Specificity
    Chemical Substances Neoplasm Proteins ; Acyltransferases (EC 2.3.-)
    Language English
    Publishing date 2018-09-19
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.15252/embr.201846666
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: A ZDHHC5-GOLGA7 Protein Acyltransferase Complex Promotes Nonapoptotic Cell Death.

    Ko, Pin-Joe / Woodrow, Claire / Dubreuil, Michael M / Martin, Brent R / Skouta, Rachid / Bassik, Michael C / Dixon, Scott J

    Cell chemical biology

    2019  Volume 26, Issue 12, Page(s) 1716–1724.e9

    Abstract: Lethal small molecules are useful probes to discover and characterize novel cell death pathways and biochemical mechanisms. Here we report that the synthetic oxime-containing small molecule caspase-independent lethal 56 (CIL56) induces an unconventional ... ...

    Abstract Lethal small molecules are useful probes to discover and characterize novel cell death pathways and biochemical mechanisms. Here we report that the synthetic oxime-containing small molecule caspase-independent lethal 56 (CIL56) induces an unconventional form of nonapoptotic cell death distinct from necroptosis, ferroptosis, and other pathways. CIL56-induced cell death requires a catalytically active protein S-acyltransferase complex comprising the enzyme ZDHHC5 and an accessory subunit GOLGA7. The ZDHHC5-GOLGA7 complex is mutually stabilizing and localizes to the plasma membrane. CIL56 inhibits anterograde protein transport from the Golgi apparatus, which may be lethal in the context of ongoing ZDHHC5-GOLGA7 complex-dependent retrograde protein trafficking from the plasma membrane to internal sites. Other oxime-containing small molecules, structurally distinct from CIL56, may trigger cell death through the same pathway. These results define an unconventional form of nonapoptotic cell death regulated by protein S-acylation.
    MeSH term(s) Acylation ; Acyltransferases/chemistry ; Acyltransferases/genetics ; Acyltransferases/metabolism ; Animals ; Cell Death/drug effects ; Cell Line ; Cell Membrane/metabolism ; Fused-Ring Compounds/chemistry ; Fused-Ring Compounds/pharmacology ; Golgi Apparatus/drug effects ; Golgi Apparatus/metabolism ; Golgi Apparatus/ultrastructure ; Golgi Matrix Proteins/chemistry ; Golgi Matrix Proteins/genetics ; Golgi Matrix Proteins/metabolism ; Humans ; Mice ; Oximes/chemistry ; Oximes/pharmacology ; Protein S/metabolism ; Protein Transport/drug effects
    Chemical Substances Fused-Ring Compounds ; GOLGA7 protein, human ; Golgi Matrix Proteins ; Oximes ; Protein S ; caspase-independent lethal 56 ; Acyltransferases (EC 2.3.-) ; ZDHHC5 protein, human (EC 2.3.1.225)
    Language English
    Publishing date 2019-10-17
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 2451-9448
    ISSN (online) 2451-9448
    DOI 10.1016/j.chembiol.2019.09.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Exogenous Monounsaturated Fatty Acids Promote a Ferroptosis-Resistant Cell State.

    Magtanong, Leslie / Ko, Pin-Joe / To, Milton / Cao, Jennifer Yinuo / Forcina, Giovanni C / Tarangelo, Amy / Ward, Carl C / Cho, Kevin / Patti, Gary J / Nomura, Daniel K / Olzmann, James A / Dixon, Scott J

    Cell chemical biology

    2019  Volume 26, Issue 3, Page(s) 420–432.e9

    Abstract: The initiation and execution of cell death can be regulated by various lipids. How the levels of environmental (exogenous) lipids impact cell death sensitivity is not well understood. We find that exogenous monounsaturated fatty acids (MUFAs) potently ... ...

    Abstract The initiation and execution of cell death can be regulated by various lipids. How the levels of environmental (exogenous) lipids impact cell death sensitivity is not well understood. We find that exogenous monounsaturated fatty acids (MUFAs) potently inhibit the non-apoptotic, iron-dependent, oxidative cell death process of ferroptosis. This protective effect is associated with the suppression of lipid reactive oxygen species (ROS) accumulation at the plasma membrane and decreased levels of phospholipids containing oxidizable polyunsaturated fatty acids. Treatment with exogenous MUFAs reduces the sensitivity of plasma membrane lipids to oxidation over several hours. This effect requires MUFA activation by acyl-coenzyme A synthetase long-chain family member 3 (ACSL3) and is independent of lipid droplet formation. Exogenous MUFAs also protect cells from apoptotic lipotoxicity caused by the accumulation of saturated fatty acids, but in an ACSL3-independent manner. Our work demonstrates that ACSL3-dependent MUFA activation promotes a ferroptosis-resistant cell state.
    MeSH term(s) Animals ; Arachidonic Acid/chemistry ; Arachidonic Acid/metabolism ; Arachidonic Acid/pharmacology ; Cell Line ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Coenzyme A Ligases/metabolism ; Fatty Acids, Monounsaturated/chemistry ; Fatty Acids, Monounsaturated/metabolism ; Fatty Acids, Monounsaturated/pharmacology ; Ferroptosis/drug effects ; Lipid Droplets/chemistry ; Lipid Droplets/metabolism ; Lipids/chemistry ; Mice ; Oxidation-Reduction ; Phospholipid Hydroperoxide Glutathione Peroxidase/genetics ; Phospholipid Hydroperoxide Glutathione Peroxidase/metabolism ; Reactive Oxygen Species/chemistry ; Reactive Oxygen Species/metabolism
    Chemical Substances Fatty Acids, Monounsaturated ; Lipids ; Reactive Oxygen Species ; Arachidonic Acid (27YG812J1I) ; Phospholipid Hydroperoxide Glutathione Peroxidase (EC 1.11.1.12) ; glutathione peroxidase 4, mouse (EC 1.11.1.9) ; Acsl3 protein, mouse (EC 6.1.2.3) ; Coenzyme A Ligases (EC 6.2.1.-)
    Language English
    Publishing date 2019-01-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 2451-9448
    ISSN (online) 2451-9448
    DOI 10.1016/j.chembiol.2018.11.016
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Transient knockdown and overexpression reveal a developmental role for the zebrafish enosf1b gene

    Finckbeiner Steve / Ko Pin-Joe / Carrington Blake / Sood Raman / Gross Kenneth / Dolnick Bruce / Sufrin Janice / Liu Paul

    Cell & Bioscience, Vol 1, Iss 1, p

    2011  Volume 32

    Abstract: Abstract Background Despite detailed in vivo knowledge of glycolytic enolases and many bacterial non-enolase members of the superfamily, little is known about the in vivo function of vertebrate non-enolase enolase superfamily members (ENOSF1s). Results ... ...

    Abstract Abstract Background Despite detailed in vivo knowledge of glycolytic enolases and many bacterial non-enolase members of the superfamily, little is known about the in vivo function of vertebrate non-enolase enolase superfamily members (ENOSF1s). Results of previous studies suggest involvement of the β splice form of ENOSF1 in breast and colon cancers. This study used the zebrafish ( Danio rerio ) as a vertebrate model of ENOSF1β function. Results Whole mount in situ hybridization (WISH) showed that zebrafish ENOSF1β ( enosf1b ) is zygotic and expressed ubiquitously through the first 24 hours post fertilization (hpf). After 24 hpf, enosf1b expression is restricted to the notochord. Embryos injected with enosf1b -EGFP mRNA grew slower than EGFP mRNA-injected embryos but caught up to the EGFP-injected embryos by 48 hpf. Embryos injected with ATG or exon 10 enosf1b mRNA-targeting morpholinos had kinked notochords, shortened anterior-posterior axes, and circulatory edema. WISH for ntl or pax2a expression showed that embryos injected with either morpholino have deformed notochord and pronephros. TUNEL staining revealed increased apoptosis in the peri-notochord region. Conclusions This study is the first report of ENOSF1 function in a vertebrate and shows that ENOSF1 is required for embryonic development. Increased apoptosis following enosf1b knockdown suggests a potential survival advantage for increased ENOSF1β expression in human cancers.
    Keywords Biotechnology ; TP248.13-248.65 ; Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
    Language English
    Publishing date 2011-09-01T00:00:00Z
    Publisher BMC
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Transient knockdown and overexpression reveal a developmental role for the zebrafish enosf1b gene.

    Finckbeiner, Steve / Ko, Pin-Joe / Carrington, Blake / Sood, Raman / Gross, Kenneth / Dolnick, Bruce / Sufrin, Janice / Liu, Paul

    Cell & bioscience

    2011  Volume 1, Page(s) 32

    Abstract: Background: Despite detailed in vivo knowledge of glycolytic enolases and many bacterial non-enolase members of the superfamily, little is known about the in vivo function of vertebrate non-enolase enolase superfamily members (ENOSF1s). Results of ... ...

    Abstract Background: Despite detailed in vivo knowledge of glycolytic enolases and many bacterial non-enolase members of the superfamily, little is known about the in vivo function of vertebrate non-enolase enolase superfamily members (ENOSF1s). Results of previous studies suggest involvement of the β splice form of ENOSF1 in breast and colon cancers. This study used the zebrafish (Danio rerio) as a vertebrate model of ENOSF1β function.
    Results: Whole mount in situ hybridization (WISH) showed that zebrafish ENOSF1β (enosf1b) is zygotic and expressed ubiquitously through the first 24 hours post fertilization (hpf). After 24 hpf, enosf1b expression is restricted to the notochord. Embryos injected with enosf1b-EGFP mRNA grew slower than EGFP mRNA-injected embryos but caught up to the EGFP-injected embryos by 48 hpf. Embryos injected with ATG or exon 10 enosf1b mRNA-targeting morpholinos had kinked notochords, shortened anterior-posterior axes, and circulatory edema. WISH for ntl or pax2a expression showed that embryos injected with either morpholino have deformed notochord and pronephros. TUNEL staining revealed increased apoptosis in the peri-notochord region.
    Conclusions: This study is the first report of ENOSF1 function in a vertebrate and shows that ENOSF1 is required for embryonic development. Increased apoptosis following enosf1b knockdown suggests a potential survival advantage for increased ENOSF1β expression in human cancers.
    Language English
    Publishing date 2011-09-26
    Publishing country England
    Document type Journal Article
    ZDB-ID 2593367-X
    ISSN 2045-3701 ; 2045-3701
    ISSN (online) 2045-3701
    ISSN 2045-3701
    DOI 10.1186/2045-3701-1-32
    Database MEDical Literature Analysis and Retrieval System OnLINE

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