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  1. Article: Editorial: Yeast Differentiation: From Cell-to-Cell Heterogeneity to Replicative Aging and Regulated Cell Death.

    Hardwick, J Marie / Knorre, Dmitry / Palkova, Zdena / Winderickx, Joris

    Frontiers in cell and developmental biology

    2022  Volume 9, Page(s) 823447

    Language English
    Publishing date 2022-01-04
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2021.823447
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Yeasts as Complementary Model Systems for the Study of the Pathological Repercussions of Enhanced Synphilin-1 Glycation and Oxidation.

    Seynnaeve, David / Mulvihill, Daniel P / Winderickx, Joris / Franssens, Vanessa

    International journal of molecular sciences

    2021  Volume 22, Issue 4

    Abstract: Synphilin-1 has previously been identified as an interaction partner of α-Synuclein (αSyn), a primary constituent of neurodegenerative disease-linked Lewy bodies. In this study, the repercussions of a disrupted glyoxalase system and aldose reductase ... ...

    Abstract Synphilin-1 has previously been identified as an interaction partner of α-Synuclein (αSyn), a primary constituent of neurodegenerative disease-linked Lewy bodies. In this study, the repercussions of a disrupted glyoxalase system and aldose reductase function on Synphilin-1 inclusion formation characteristics and cell growth were investigated. To this end, either fluorescent dsRed-tagged or non-tagged human
    MeSH term(s) Alcohol Oxidoreductases/genetics ; Alcohol Oxidoreductases/metabolism ; Aldehyde Reductase/antagonists & inhibitors ; Aldehyde Reductase/genetics ; Aldehyde Reductase/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Glycosylation ; Humans ; Inclusion Bodies ; Lactoylglutathione Lyase/antagonists & inhibitors ; Lactoylglutathione Lyase/genetics ; Lactoylglutathione Lyase/metabolism ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/metabolism ; Oxidation-Reduction ; Oxidative Stress ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Carrier Proteins ; Nerve Tissue Proteins ; SNCAIP protein, human ; Saccharomyces cerevisiae Proteins ; Alcohol Oxidoreductases (EC 1.1.-) ; Aldehyde Reductase (EC 1.1.1.21) ; gluconolactone oxidase (EC 1.1.3.-) ; Lactoylglutathione Lyase (EC 4.4.1.5)
    Language English
    Publishing date 2021-02-07
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms22041677
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Coordinated glucose-induced Ca

    Ma, Tien-Yang / Deprez, Marie-Anne / Callewaert, Geert / Winderickx, Joris

    Cell calcium

    2021  Volume 100, Page(s) 102479

    Abstract: ... ...

    Abstract Ca
    MeSH term(s) Glucose ; Hydrogen-Ion Concentration ; Proton-Translocating ATPases/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Vacuolar Proton-Translocating ATPases ; Vacuoles/metabolism
    Chemical Substances Saccharomyces cerevisiae Proteins ; Vacuolar Proton-Translocating ATPases (EC 3.6.1.-) ; Proton-Translocating ATPases (EC 3.6.3.14) ; Glucose (IY9XDZ35W2)
    Language English
    Publishing date 2021-09-26
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 757687-0
    ISSN 1532-1991 ; 0143-4160
    ISSN (online) 1532-1991
    ISSN 0143-4160
    DOI 10.1016/j.ceca.2021.102479
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1596: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: The Yeast Protein Kinase Sch9 Functions as a Central Nutrient-Responsive Hub That Calibrates Metabolic and Stress-Related Responses.

    Caligaris, Marco / Sampaio-Marques, Belém / Hatakeyama, Riko / Pillet, Benjamin / Ludovico, Paula / De Virgilio, Claudio / Winderickx, Joris / Nicastro, Raffaele

    Journal of fungi (Basel, Switzerland)

    2023  Volume 9, Issue 8

    Abstract: Yeast cells are equipped with different nutrient signaling pathways that enable them to sense the availability of various nutrients and adjust metabolism and growth accordingly. These pathways are part of an intricate network since most of them are cross- ...

    Abstract Yeast cells are equipped with different nutrient signaling pathways that enable them to sense the availability of various nutrients and adjust metabolism and growth accordingly. These pathways are part of an intricate network since most of them are cross-regulated and subject to feedback regulation at different levels. In yeast, a central role is played by Sch9, a protein kinase that functions as a proximal effector of the conserved growth-regulatory TORC1 complex to mediate information on the availability of free amino acids. However, recent studies established that Sch9 is more than a TORC1-effector as its activity is tuned by several other kinases. This allows Sch9 to function as an integrator that aligns different input signals to achieve accuracy in metabolic responses and stress-related molecular adaptations. In this review, we highlight the latest findings on the structure and regulation of Sch9, as well as its role as a nutrient-responsive hub that impacts on growth and longevity of yeast cells. Given that most key players impinging on Sch9 are well-conserved, we also discuss how studies on Sch9 can be instrumental to further elucidate mechanisms underpinning healthy aging in mammalians.
    Language English
    Publishing date 2023-07-26
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2784229-0
    ISSN 2309-608X ; 2309-608X
    ISSN (online) 2309-608X
    ISSN 2309-608X
    DOI 10.3390/jof9080787
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: The Role of Sch9 and the V-ATPase in the Adaptation Response to Acetic Acid and the Consequences for Growth and Chronological Lifespan

    Deprez, Marie-Anne / Maertens, Jeroen M. / Olsson, Lisbeth / Bettiga, Maurizio / Winderickx, Joris

    Microorganisms. 2021 Sept. 03, v. 9, no. 9

    2021  

    Abstract: Studies with Saccharomyces cerevisiae indicated that non-physiologically high levels of acetic acid promote cellular acidification, chronological aging, and programmed cell death. In the current study, we compared the cellular lipid composition, acetic ... ...

    Abstract Studies with Saccharomyces cerevisiae indicated that non-physiologically high levels of acetic acid promote cellular acidification, chronological aging, and programmed cell death. In the current study, we compared the cellular lipid composition, acetic acid uptake, intracellular pH, growth, and chronological lifespan of wild-type cells and mutants lacking the protein kinase Sch9 and/or a functional V-ATPase when grown in medium supplemented with different acetic acid concentrations. Our data show that strains lacking the V-ATPase are especially more susceptible to growth arrest in the presence of high acetic acid concentrations, which is due to a slower adaptation to the acid stress. These V-ATPase mutants also displayed changes in lipid homeostasis, including alterations in their membrane lipid composition that influences the acetic acid diffusion rate and changes in sphingolipid metabolism and the sphingolipid rheostat, which is known to regulate stress tolerance and longevity of yeast cells. However, we provide evidence that the supplementation of 20 mM acetic acid has a cytoprotective and presumable hormesis effect that extends the longevity of all strains tested, including the V-ATPase compromised mutants. We also demonstrate that the long-lived sch9Δ strain itself secretes significant amounts of acetic acid during stationary phase, which in addition to its enhanced accumulation of storage lipids may underlie its increased lifespan.
    Keywords H-transporting ATP synthase ; Saccharomyces cerevisiae ; acetic acid ; acidification ; homeostasis ; hormesis ; lipid composition ; longevity ; pH ; programmed cell death ; protein kinases ; sphingolipids ; stress tolerance ; yeasts
    Language English
    Dates of publication 2021-0903
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2720891-6
    ISSN 2076-2607
    ISSN 2076-2607
    DOI 10.3390/microorganisms9091871
    Database NAL-Catalogue (AGRICOLA)

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  6. Article: The Role of Sch9 and the V-ATPase in the Adaptation Response to Acetic Acid and the Consequences for Growth and Chronological Lifespan.

    Deprez, Marie-Anne / Maertens, Jeroen M / Olsson, Lisbeth / Bettiga, Maurizio / Winderickx, Joris

    Microorganisms

    2021  Volume 9, Issue 9

    Abstract: ... Studies ... ...

    Abstract Studies with
    Language English
    Publishing date 2021-09-03
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2720891-6
    ISSN 2076-2607
    ISSN 2076-2607
    DOI 10.3390/microorganisms9091871
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: A Mitochondria-Associated Oxidative Stress Perspective on Huntington's Disease.

    Zheng, Ju / Winderickx, Joris / Franssens, Vanessa / Liu, Beidong

    Frontiers in molecular neuroscience

    2018  Volume 11, Page(s) 329

    Abstract: Huntington's disease (HD) is genetically caused by mutation of the Huntingtin ( ...

    Abstract Huntington's disease (HD) is genetically caused by mutation of the Huntingtin (
    Language English
    Publishing date 2018-09-19
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2452967-9
    ISSN 1662-5099
    ISSN 1662-5099
    DOI 10.3389/fnmol.2018.00329
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  8. Article: Inter-organellar Communication in Parkinson's and Alzheimer's Disease: Looking Beyond Endoplasmic Reticulum-Mitochondria Contact Sites.

    Vrijsen, Stephanie / Vrancx, Céline / Del Vecchio, Mara / Swinnen, Johannes V / Agostinis, Patrizia / Winderickx, Joris / Vangheluwe, Peter / Annaert, Wim

    Frontiers in neuroscience

    2022  Volume 16, Page(s) 900338

    Abstract: Neurodegenerative diseases (NDs) are generally considered proteinopathies but whereas this may initiate disease in familial cases, onset in sporadic diseases may originate from a gradually disrupted organellar homeostasis. Herein, endolysosomal ... ...

    Abstract Neurodegenerative diseases (NDs) are generally considered proteinopathies but whereas this may initiate disease in familial cases, onset in sporadic diseases may originate from a gradually disrupted organellar homeostasis. Herein, endolysosomal abnormalities, mitochondrial dysfunction, endoplasmic reticulum (ER) stress, and altered lipid metabolism are commonly observed in early preclinical stages of major NDs, including Parkinson's disease (PD) and Alzheimer's disease (AD). Among the multitude of underlying defective molecular mechanisms that have been suggested in the past decades, dysregulation of inter-organellar communication through the so-called membrane contact sites (MCSs) is becoming increasingly apparent. Although MCSs exist between almost every other type of subcellular organelle, to date, most focus has been put on defective communication between the ER and mitochondria in NDs, given these compartments are critical in neuronal survival. Contributions of other MCSs, notably those with endolysosomes and lipid droplets are emerging, supported as well by genetic studies, identifying genes functionally involved in lysosomal homeostasis. In this review, we summarize the molecular identity of the organelle interactome in yeast and mammalian cells, and critically evaluate the evidence supporting the contribution of disturbed MCSs to the general disrupted inter-organellar homeostasis in NDs, taking PD and AD as major examples.
    Language English
    Publishing date 2022-06-21
    Publishing country Switzerland
    Document type Systematic Review
    ZDB-ID 2411902-7
    ISSN 1662-453X ; 1662-4548
    ISSN (online) 1662-453X
    ISSN 1662-4548
    DOI 10.3389/fnins.2022.900338
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: The nutrient-responsive CDK Pho85 primes the Sch9 kinase for its activation by TORC1.

    Deprez, Marie-Anne / Caligaris, Marco / Rosseels, Joëlle / Hatakeyama, Riko / Ghillebert, Ruben / Sampaio-Marques, Belém / Mudholkar, Kaivalya / Eskes, Elja / Meert, Els / Ungermann, Christian / Ludovico, Paula / Rospert, Sabine / De Virgilio, Claudio / Winderickx, Joris

    PLoS genetics

    2023  Volume 19, Issue 2, Page(s) e1010641

    Abstract: Yeast cells maintain an intricate network of nutrient signaling pathways enabling them to integrate information on the availability of different nutrients and adjust their metabolism and growth accordingly. Cells that are no longer capable of integrating ...

    Abstract Yeast cells maintain an intricate network of nutrient signaling pathways enabling them to integrate information on the availability of different nutrients and adjust their metabolism and growth accordingly. Cells that are no longer capable of integrating this information, or that are unable to make the necessary adaptations, will cease growth and eventually die. Here, we studied the molecular basis underlying the synthetic lethality caused by loss of the protein kinase Sch9, a key player in amino acid signaling and proximal effector of the conserved growth-regulatory TORC1 complex, when combined with either loss of the cyclin-dependent kinase (CDK) Pho85 or loss of its inhibitor Pho81, which both have pivotal roles in phosphate sensing and cell cycle regulation. We demonstrate that it is specifically the CDK-cyclin pair Pho85-Pho80 or the partially redundant CDK-cyclin pairs Pho85-Pcl6/Pcl7 that become essential for growth when Sch9 is absent. Interestingly, the respective three CDK-cyclin pairs regulate the activity and distribution of the phosphatidylinositol-3 phosphate 5-kinase Fab1 on endosomes and vacuoles, where it generates phosphatidylinositol-3,5 bisphosphate that serves to recruit both TORC1 and its substrate Sch9. In addition, Pho85-Pho80 directly phosphorylates Sch9 at Ser726, and to a lesser extent at Thr723, thereby priming Sch9 for its subsequent phosphorylation and activation by TORC1. The TORC1-Sch9 signaling branch therefore integrates Pho85-mediated information at different levels. In this context, we also discovered that loss of the transcription factor Pho4 rescued the synthetic lethality caused by loss of Pho85 and Sch9, indicating that both signaling pathways also converge on Pho4, which appears to be wired to a feedback loop involving the high-affinity phosphate transporter Pho84 that fine-tunes Sch9-mediated responses.
    MeSH term(s) Cyclin-Dependent Kinases/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Repressor Proteins/metabolism ; Mechanistic Target of Rapamycin Complex 1/genetics ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Cyclins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Phosphates/metabolism ; Phosphatidylinositols/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Protein Serine-Threonine Kinases/metabolism
    Chemical Substances Cyclin-Dependent Kinases (EC 2.7.11.22) ; Saccharomyces cerevisiae Proteins ; Repressor Proteins ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Cyclins ; Phosphates ; Phosphatidylinositols ; PHO85 protein, S cerevisiae (EC 2.7.11.22) ; FAB1 protein, S cerevisiae (EC 2.7.1.-) ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; SCH9 protein, S cerevisiae (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2023-02-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2186725-2
    ISSN 1553-7404 ; 1553-7390
    ISSN (online) 1553-7404
    ISSN 1553-7390
    DOI 10.1371/journal.pgen.1010641
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Snf1/AMPK fine-tunes TORC1 signaling in response to glucose starvation.

    Caligaris, Marco / Nicastro, Raffaele / Hu, Zehan / Tripodi, Farida / Hummel, Johannes Erwin / Pillet, Benjamin / Deprez, Marie-Anne / Winderickx, Joris / Rospert, Sabine / Coccetti, Paola / Dengjel, Jörn / De Virgilio, Claudio

    eLife

    2023  Volume 12

    Abstract: The AMP-activated protein kinase (AMPK) and the target of rapamycin complex 1 (TORC1) are central kinase modules of two opposing signaling pathways that control eukaryotic cell growth and metabolism in response to the availability of energy and nutrients. ...

    Abstract The AMP-activated protein kinase (AMPK) and the target of rapamycin complex 1 (TORC1) are central kinase modules of two opposing signaling pathways that control eukaryotic cell growth and metabolism in response to the availability of energy and nutrients. Accordingly, energy depletion activates AMPK to inhibit growth, while nutrients and high energy levels activate TORC1 to promote growth. Both in mammals and lower eukaryotes such as yeast, the AMPK and TORC1 pathways are wired to each other at different levels, which ensures homeostatic control of growth and metabolism. In this context, a previous study (Hughes Hallett et al., 2015) reported that AMPK in yeast, that is Snf1, prevents the transient TORC1 reactivation during the early phase following acute glucose starvation, but the underlying mechanism has remained elusive. Using a combination of unbiased mass spectrometry (MS)-based phosphoproteomics, genetic, biochemical, and physiological experiments, we show here that Snf1 temporally maintains TORC1 inactive in glucose-starved cells primarily through the TORC1-regulatory protein Pib2. Our data, therefore, extend the function of Pib2 to a hub that integrates both glucose and, as reported earlier, glutamine signals to control TORC1. We further demonstrate that Snf1 phosphorylates the TORC1 effector kinase Sch9 within its N-terminal region and thereby antagonizes the phosphorylation of a C-terminal TORC1-target residue within Sch9 itself that is critical for its activity. The consequences of Snf1-mediated phosphorylation of Pib2 and Sch9 are physiologically additive and sufficient to explain the role of Snf1 in short-term inhibition of TORC1 in acutely glucose-starved cells.
    MeSH term(s) Animals ; AMP-Activated Protein Kinases/metabolism ; Glucose/metabolism ; Mammals/metabolism ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances AMP-Activated Protein Kinases (EC 2.7.11.31) ; Glucose (IY9XDZ35W2) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Saccharomyces cerevisiae Proteins ; SNF1-related protein kinases (EC 2.7.1.-)
    Language English
    Publishing date 2023-02-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.84319
    Database MEDical Literature Analysis and Retrieval System OnLINE

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