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  1. Article ; Online: Crosstalk between cystine and glutathione is critical for the regulation of amino acid signaling pathways and ferroptosis.

    Yu, Xinlei / Long, Yun Chau

    Scientific reports

    2016  Volume 6, Page(s) 30033

    Abstract: Although essential amino acids regulate mechanistic target of rapamycin complex 1 (mTORC1) and the integrated stress response (ISR), the role of cysteine is unknown. We found that in hepatoma HepG2 cells, cystine (oxidized form of cysteine) activated ... ...

    Abstract Although essential amino acids regulate mechanistic target of rapamycin complex 1 (mTORC1) and the integrated stress response (ISR), the role of cysteine is unknown. We found that in hepatoma HepG2 cells, cystine (oxidized form of cysteine) activated mTORC1 and suppressed the ISR. Cystine deprivation induced GSH efflux and extracellular degradation, which aimed to restore cellular cysteine. Inhibition of γ-glutamyl transpeptidase (GGT) impaired the ability of GSH or cell-permeable GSH to restore mTORC1 signaling and the ISR, suggesting that the capacity of GSH to release cysteine, but not GSH per se, regulated the signaling networks. Inhibition of protein translation restored both mTORC1 signaling and the ISR during cystine starvation, suggesting the bulk of cellular cysteine was committed to the biosynthetic process. Cellular cysteine and GSH displayed overlapping protective roles in the suppression of ferroptosis, further supporting their cooperation in the regulation of cell signaling. Thus, cellular cysteine and its derivative GSH cooperate to regulate mTORC1 pathway, the ISR and ferroptosis.
    Language English
    Publishing date 2016-07-18
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep30033
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  2. Article ; Online: Downregulation of Diacylglycerol Kinase Delta Contributes to Hyperglycemia-Induced Insulin Resistance.

    Chibalin, Alexander V / Leng, Ying / Vieira, Elaine / Krook, Anna / Björnholm, Marie / Long, Yun Chau / Kotova, Olga / Zhong, Zhihui / Sakane, Fumio / Steiler, Tatiana / Nylén, Carolina / Wang, Jianjun / Laakso, Markku / Topham, Matthew K / Gilbert, Marc / Wallberg-Henriksson, Harriet / Zierath, Juleen R

    Cell

    2022  Volume 185, Issue 2, Page(s) 397–398

    Language English
    Publishing date 2022-01-21
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2021.12.044
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  3. Article ; Online: Skeletal muscle AMP kinase as a target to prevent pathogenesis of Type 2 diabetes.

    Krook, Anna / Long, Yun Chau / Zierath, Juleen R

    Expert review of endocrinology & metabolism

    2018  Volume 2, Issue 4, Page(s) 477–485

    Abstract: The metabolic property of skeletal muscle is highly malleable and adapts to various physiological demands by shifting energy-substrate metabolism. Skeletal muscle metabolism has a significant impact on whole-body metabolism and substrate utilization. ... ...

    Abstract The metabolic property of skeletal muscle is highly malleable and adapts to various physiological demands by shifting energy-substrate metabolism. Skeletal muscle metabolism has a significant impact on whole-body metabolism and substrate utilization. Glucose and lipids are the main oxidative fuel substrates in skeletal muscle, and their utilization is coordinated by complex regulatory mechanisms. In people with Type 2 diabetes, glucose uptake and lipid oxidation in skeletal muscle are impaired. These metabolic defects are coupled to impaired insulin signaling. Exercise increases glucose uptake and lipid oxidation by an insulin-independent mechanism. The AMP-activated protein kinase (AMPK) cascade is activated in response to metabolic stress and has therefore been implicated in the regulation of exercise-induced metabolic and gene regulatory responses. AMPK is a heterotrimeric complex composed of a catalytic α, and regulatory β and γ subunits. Selective regulation of AMPK in skeletal muscle may be achieved by targeting α1/β2/γ3 heterotrimeric complexes. Activation of AMPK enhances GLUT4 translocation of glucose uptake in skeletal muscle from Type 2 diabetic patients and animal models of the disease by an insulin-independent mechanism. Transgenic overexpression of mutated forms of the AMPK γ3 subunit provide evidence that activation of AMPK promotes lipid oxidation and prevents the development of skeletal muscle insulin resistance. Thus, AMPK provides a molecular entry point into novel regulatory pathways to enhance lipid and glucose metabolism in an effort to prevent and treat skeletal muscle insulin resistance associated with Type 2 diabetes.
    Language English
    Publishing date 2018-10-05
    Publishing country England
    Document type Journal Article
    ISSN 1744-8417
    ISSN (online) 1744-8417
    DOI 10.1586/17446651.2.4.477
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  4. Article ; Online: Correction for Long et al., "Insulin Receptor Substrates Irs1 and Irs2 Coordinate Skeletal Muscle Growth and Metabolism via the Akt and AMPK Pathways".

    Long, Yun Chau / Cheng, Zhiyong / Copps, Kyle D / White, Morris F

    Molecular and cellular biology

    2017  Volume 37, Issue 15

    Language English
    Publishing date 2017-07-14
    Publishing country United States
    Document type Journal Article ; Published Erratum
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00232-17
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    Zs.A 1666: Show issues Location:
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  5. Article ; Online: Autophagy modulates amino acid signaling network in myotubes: differential effects on mTORC1 pathway and the integrated stress response.

    Yu, Xinlei / Long, Yun Chau

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology

    2015  Volume 29, Issue 2, Page(s) 394–407

    Abstract: Induction of autophagy and the integrated stress response is important for amino acid homeostasis. It remains unknown whether the autophagy coregulates both mechanistic target of rapamycin complex 1 (mTORC1) signaling and the integrated stress response. ... ...

    Abstract Induction of autophagy and the integrated stress response is important for amino acid homeostasis. It remains unknown whether the autophagy coregulates both mechanistic target of rapamycin complex 1 (mTORC1) signaling and the integrated stress response. In mouse C2C12 myotubes, we found that amino acid limitation induced autophagy and that the subsequent release of amino acid is required to sustain mTORC1 signaling. Inhibition of autophagy by bafilomycin A1 or chloroquine treatment during amino acid scarcity abolished mTORC1 signaling, an effect that could be rescued by inhibiting protein synthesis or amino acid supplementation, respectively. Autophagy is required to sustain the balance of both essential and nonessential amino acids during amino acid starvation, and it has a predominant role over the ubiquitin-proteasome system in the regulation of mTORC1. Inhibition of autophagy was found to activate the integrated stress response, as well as eukaryotic initiation factor 2α (eIF2α) and its target genes independent of amino acid availability. Conversely, autophagy induction via mTOR inhibition is sufficient to reduce eIF2α phosphorylation. Thus, autophagy protects the eIF2α-mediated stress response independent of amino acid supply in cultured myotubes. Our results showed that autophagy uniquely modulates mTORC1 and the integrated stress response in an amino acid-dependent and -independent manner, respectively.
    MeSH term(s) Amino Acids/metabolism ; Animals ; Autophagy ; Cell Line ; Chloroquine/chemistry ; Eukaryotic Initiation Factor-2/metabolism ; Green Fluorescent Proteins/metabolism ; Homeostasis ; Lysosomes/metabolism ; Macrolides/chemistry ; Mechanistic Target of Rapamycin Complex 1 ; Mice ; Multiprotein Complexes/metabolism ; Muscle, Skeletal/metabolism ; Phosphorylation ; Proteasome Endopeptidase Complex/metabolism ; Signal Transduction ; TOR Serine-Threonine Kinases/metabolism ; Ubiquitin/metabolism
    Chemical Substances Amino Acids ; Eukaryotic Initiation Factor-2 ; Macrolides ; Multiprotein Complexes ; Ubiquitin ; Green Fluorescent Proteins (147336-22-9) ; Chloroquine (886U3H6UFF) ; bafilomycin A1 (88899-55-2) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2015-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 639186-2
    ISSN 1530-6860 ; 0892-6638
    ISSN (online) 1530-6860
    ISSN 0892-6638
    DOI 10.1096/fj.14-252841
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    Zs.A 2266: Show issues Location:
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    Zs.MO 296: Show issues

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  6. Article ; Online: Npac Is A Co-factor of Histone H3K36me3 and Regulates Transcriptional Elongation in Mouse Embryonic Stem Cells

    Sue Yu / Jia Li / Guanxu Ji / Zhen Long Ng / Jiamin Siew / Wan Ning Lo / Ying Ye / Yuan Yuan Chew / Yun Chau Long / Wensheng Zhang / Ernesto Guccione / Yuin Han Loh / Zhi-Hong Jiang / Henry Yang / Qiang Wu

    Genomics, Proteomics & Bioinformatics, Vol 20, Iss 1, Pp 110-

    2022  Volume 128

    Abstract: Chromatin modification contributes to pluripotency maintenance in embryonic stem cells (ESCs). However, the related mechanisms remain obscure. Here, we show that Npac, a “reader” of histone H3 lysine 36 trimethylation (H3K36me3), is required to maintain ... ...

    Abstract Chromatin modification contributes to pluripotency maintenance in embryonic stem cells (ESCs). However, the related mechanisms remain obscure. Here, we show that Npac, a “reader” of histone H3 lysine 36 trimethylation (H3K36me3), is required to maintain mouse ESC (mESC) pluripotency since knockdown of Npac causes mESC differentiation. Depletion of Npac in mouse embryonic fibroblasts (MEFs) inhibits reprogramming efficiency. Furthermore, our chromatin immunoprecipitation followed by sequencing (ChIP-seq) results of Npac reveal that Npac co-localizes with histone H3K36me3 in gene bodies of actively transcribed genes in mESCs. Interestingly, we find that Npac interacts with positive transcription elongation factor b (p-TEFb), Ser2-phosphorylated RNA Pol II (RNA Pol II Ser2P), and Ser5-phosphorylated RNA Pol II (RNA Pol II Ser5P). Furthermore, depletion of Npac disrupts transcriptional elongation of the pluripotency genes Nanog and Rif1. Taken together, we propose that Npac is essential for the transcriptional elongation of pluripotency genes by recruiting p-TEFb and interacting with RNA Pol II Ser2P and Ser5P.
    Keywords Npac ; Pluripotency ; Reprogramming ; Histone H3K36me3 ; Transcriptional elongation ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2022-02-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
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  7. Article ; Online: Glutamine metabolism regulates autophagy-dependent mTORC1 reactivation during amino acid starvation.

    Tan, Hayden Weng Siong / Sim, Arthur Yi Loong / Long, Yun Chau

    Nature communications

    2017  Volume 8, Issue 1, Page(s) 338

    Abstract: Activation of autophagy and elevation of glutamine synthesis represent key adaptations to maintain amino acid balance during starvation. In this study, we investigate the role of autophagy and glutamine on the regulation of mTORC1, a critical kinase that ...

    Abstract Activation of autophagy and elevation of glutamine synthesis represent key adaptations to maintain amino acid balance during starvation. In this study, we investigate the role of autophagy and glutamine on the regulation of mTORC1, a critical kinase that regulates cell growth and proliferation. We report that supplementation of glutamine alone is sufficient to restore mTORC1 activity during prolonged amino acid starvation. Inhibition of autophagy abolishes the restorative effect of glutamine, suggesting that reactivation of mTORC1 is autophagy-dependent. Inhibition of glutaminolysis or transamination impairs glutamine-mediated mTORC1 reactivation, suggesting glutamine reactivates mTORC1 specifically through its conversion to glutamate and restoration of non-essential amino acid pool. Despite a persistent drop in essential amino acid pool during amino acid starvation, crosstalk between glutamine and autophagy is sufficient to restore insulin sensitivity of mTORC1. Thus, glutamine metabolism and autophagy constitute a specific metabolic program which restores mTORC1 activity during amino acid starvation.mTORC1 is a critical kinase that regulates cell growth and proliferation. Here the authors show that glutamine metabolism is sufficient to restore mTORC1 activity during prolonged amino acid starvation in an autophagy-dependent manner.
    Language English
    Publishing date 2017--24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2041-1723
    ISSN (online) 2041-1723
    DOI 10.1038/s41467-017-00369-y
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  8. Article ; Online: Glutamine metabolism regulates autophagy-dependent mTORC1 reactivation during amino acid starvation

    Hayden Weng Siong Tan / Arthur Yi Loong Sim / Yun Chau Long

    Nature Communications, Vol 8, Iss 1, Pp 1-

    2017  Volume 10

    Abstract: mTORC1 is a critical kinase that regulates cell growth and proliferation. Here the authors show that glutamine metabolism is sufficient to restore mTORC1 activity during prolonged amino acid starvation in an autophagy-dependent manner. ...

    Abstract mTORC1 is a critical kinase that regulates cell growth and proliferation. Here the authors show that glutamine metabolism is sufficient to restore mTORC1 activity during prolonged amino acid starvation in an autophagy-dependent manner.
    Keywords Science ; Q
    Language English
    Publishing date 2017-08-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
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  9. Article ; Online: Glutamine metabolism regulates autophagy-dependent mTORC1 reactivation during amino acid starvation

    Hayden Weng Siong Tan / Arthur Yi Loong Sim / Yun Chau Long

    Nature Communications, Vol 8, Iss 1, Pp 1-

    2017  Volume 10

    Abstract: mTORC1 is a critical kinase that regulates cell growth and proliferation. Here the authors show that glutamine metabolism is sufficient to restore mTORC1 activity during prolonged amino acid starvation in an autophagy-dependent manner. ...

    Abstract mTORC1 is a critical kinase that regulates cell growth and proliferation. Here the authors show that glutamine metabolism is sufficient to restore mTORC1 activity during prolonged amino acid starvation in an autophagy-dependent manner.
    Keywords Science ; Q
    Language English
    Publishing date 2017-08-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
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  10. Article ; Online: Cysteine Deprivation Targets Ovarian Clear Cell Carcinoma

    Novera, Wisna / Lee, Zheng-Wei / Nin, Dawn Sijin / Dai, Melvin Zi-Yu / Binte Idres, Shabana / Wu, Hui / Damen, J Mirjam A / Tan, Tuan Zea / Sim, Arthur Yi Loong / Long, Yun Chau / Wu, Wei / Huang, Ruby Yun-Ju / Deng, Lih-Wen

    Antioxidants & redox signaling

    2020  Volume 33, Issue 17, Page(s) 1191–1208

    Abstract: Aims: ...

    Abstract Aims:
    MeSH term(s) Adenocarcinoma, Clear Cell/metabolism ; Apoptosis ; Cell Survival ; Cysteine/metabolism ; Female ; Ferroptosis ; Glutathione/metabolism ; Humans ; Iron/metabolism ; Mitochondria/metabolism ; Models, Biological ; Necrosis/metabolism ; Ovarian Neoplasms/metabolism ; Oxidative Stress ; Sulfur/metabolism
    Chemical Substances Sulfur (70FD1KFU70) ; Iron (E1UOL152H7) ; Glutathione (GAN16C9B8O) ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2020-05-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483836-9
    ISSN 1557-7716 ; 1523-0864
    ISSN (online) 1557-7716
    ISSN 1523-0864
    DOI 10.1089/ars.2019.7850
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    Zs.A 5488: Show issues Location:
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