LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 467

Search options

  1. Article ; Online: Lipid saturation induces degradation of squalene epoxidase for sterol homeostasis and cell survival.

    Huang, Leng-Jie / Chen, Rey-Huei

    Life science alliance

    2022  Volume 6, Issue 1

    Abstract: A fluid membrane containing a mix of unsaturated and saturated lipids is essential for life. However, it is unclear how lipid saturation might affect lipid homeostasis, membrane-associated proteins, and membrane organelles. Here, we generate temperature- ... ...

    Abstract A fluid membrane containing a mix of unsaturated and saturated lipids is essential for life. However, it is unclear how lipid saturation might affect lipid homeostasis, membrane-associated proteins, and membrane organelles. Here, we generate temperature-sensitive mutants of the sole fatty acid desaturase gene
    MeSH term(s) Squalene Monooxygenase/genetics ; Squalene Monooxygenase/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Cell Survival ; Endoplasmic Reticulum-Associated Degradation ; Saccharomyces cerevisiae/metabolism ; Homeostasis ; Sterols/metabolism ; Lipids
    Chemical Substances Squalene Monooxygenase (EC 1.14.14.17) ; Saccharomyces cerevisiae Proteins ; Sterols ; Lipids
    Language English
    Publishing date 2022-11-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2575-1077
    ISSN (online) 2575-1077
    DOI 10.26508/lsa.202201612
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  2. Article ; Online: Chromosome detachment from the nuclear envelope is required for genomic stability in closed mitosis.

    Chen, Rey-Huei

    Molecular biology of the cell

    2019  Volume 30, Issue 13, Page(s) 1578–1586

    Abstract: Mitosis in metazoans involves detachment of chromosomes from the nuclear envelope (NE) and NE breakdown, whereas yeasts maintain the nuclear structure throughout mitosis. It remains unknown how chromosome attachment to the NE might affect chromosome ... ...

    Abstract Mitosis in metazoans involves detachment of chromosomes from the nuclear envelope (NE) and NE breakdown, whereas yeasts maintain the nuclear structure throughout mitosis. It remains unknown how chromosome attachment to the NE might affect chromosome movement in yeast. By using a rapamycin-induced dimerization system to tether a specific locus of the chromosome to the NE, I found that the tethering delays the separation and causes missegregation of the region distal to the tethered site. The phenotypes are exacerbated by mutations in kinetochore components and Aurora B kinase Ipl1. The chromosome region proximal to the centromere is less affected by the tether, but it exhibits excessive oscillation before segregation. Furthermore, the tether impacts full extension of the mitotic spindle, causing abrupt shrinkage or bending of the spindle in shortened anaphase. The study supports detachment of chromosomes from the NE being required for faithful chromosome segregation in yeast and segregation of tethered chromosomes being dependent on a fully functional mitotic apparatus.
    MeSH term(s) Anaphase/physiology ; Cell Cycle Proteins/metabolism ; Centromere/metabolism ; Chromosome Segregation/physiology ; Chromosomes/genetics ; Chromosomes/physiology ; Genomic Instability/genetics ; Kinetochores/metabolism ; Mitosis/genetics ; Mitosis/physiology ; Nuclear Envelope/metabolism ; Nuclear Envelope/physiology ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Spindle Apparatus/metabolism
    Chemical Substances Cell Cycle Proteins
    Language English
    Publishing date 2019-04-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E19-02-0098
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: 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)
    Zs.MO 410: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Assembly and quality control of the protein phosphatase 1 holoenzyme involves the Cdc48-Shp1 chaperone.

    Cheng, You-Liang / Chen, Rey-Huei

    Journal of cell science

    2015  Volume 128, Issue 6, Page(s) 1180–1192

    Abstract: Protein phosphatase 1 (PP1) controls many aspects of cell physiology, which depends on its correct targeting in the cell. Nuclear localization of Glc7, the catalytic subunit of PP1 in budding yeast, requires the AAA-ATPase Cdc48 and its adaptor Shp1 ... ...

    Abstract Protein phosphatase 1 (PP1) controls many aspects of cell physiology, which depends on its correct targeting in the cell. Nuclear localization of Glc7, the catalytic subunit of PP1 in budding yeast, requires the AAA-ATPase Cdc48 and its adaptor Shp1 through an unknown mechanism. Herein, we show that mutations in SHP1 cause misfolding of Glc7 that co-aggregates with Hsp104 and Hsp42 chaperones and requires the proteasome for clearance. Mutation or depletion of the PP1 regulatory subunits Sds22 and Ypi1, which are involved in nuclear targeting of Glc7, also produce Glc7 aggregates, indicating that association with regulatory subunits stabilizes Glc7 conformation. Use of a substrate-trap Cdc48(QQ) mutant reveals that Glc7-Sds22-Ypi1 transiently associates with and is the major target of Cdc48-Shp1. Furthermore, Cdc48-Shp1 binds and prevents misfolding of PP1-like phosphatases Ppz2 and Ppq1, but not other types of phosphatases. Our data suggest that Cdc48-Shp1 functions as a molecular chaperone for the structural integrity of PP1 complex in general and that it specifically promotes the assembly of Glc7-Sds22-Ypi1 for nuclear import.
    MeSH term(s) Adenosine Triphosphatases/metabolism ; Blotting, Western ; Cell Cycle Proteins/metabolism ; Immunoprecipitation ; Intracellular Signaling Peptides and Proteins/metabolism ; Mass Spectrometry ; Molecular Chaperones/metabolism ; Protein Folding ; Protein Phosphatase 1/chemistry ; Protein Phosphatase 1/metabolism ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Valosin Containing Protein
    Chemical Substances Cell Cycle Proteins ; Intracellular Signaling Peptides and Proteins ; Molecular Chaperones ; SHP1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Ypi1 protein, S cerevisiae ; GLC7 protein, S cerevisiae (EC 3.1.3.16) ; Protein Phosphatase 1 (EC 3.1.3.16) ; Adenosine Triphosphatases (EC 3.6.1.-) ; CDC48 protein, S cerevisiae (EC 3.6.4.-) ; Valosin Containing Protein (EC 3.6.4.6)
    Language English
    Publishing date 2015-03-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.165159
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1200: 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)
    Zs.MG 14: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article: The spindle checkpoint in Xenopus laevis.

    Chen, Rey-Huei

    Frontiers in bioscience : a journal and virtual library

    2008  Volume 13, Page(s) 2231–2237

    Abstract: The spindle checkpoint ensures accurate chromosome segregation by delaying anaphase onset until all kinetochores have properly established bipolar attachment to spindle microtubules. This mechanism is important for all eukaryotic cells and is ... ...

    Abstract The spindle checkpoint ensures accurate chromosome segregation by delaying anaphase onset until all kinetochores have properly established bipolar attachment to spindle microtubules. This mechanism is important for all eukaryotic cells and is evolutionarily conserved. Much of our understanding of the molecular and biochemical mechanisms of the spindle checkpoint has been gained from parallel studies in various experimental systems. In particular, the cytoplasmic extract from the eggs of Xenopus laevis provides an unsurpassable system for biochemical analysis of the spindle checkpoint and has made important contributions to the field. This article reviews the progress of the spindle checkpoint studies in Xenopus laevis with a focus on the regulation by phosphorylation.
    MeSH term(s) Animals ; Aurora Kinases ; Cell Cycle ; Cytoplasm/metabolism ; Humans ; Kinetochores/metabolism ; MAP Kinase Signaling System ; Models, Biological ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; Spindle Apparatus/metabolism ; Xenopus laevis/genetics
    Chemical Substances Aurora Kinases (EC 2.7.11.1) ; Bub1 spindle checkpoint protein (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2008-01-01
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2141320-4
    ISSN 1093-9946
    ISSN 1093-9946
    DOI 10.2741/2837
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 5867: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article: Dual inhibition of Cdc20 by the spindle checkpoint.

    Chen, Rey-Huei

    Journal of biomedical science

    2007  Volume 14, Issue 4, Page(s) 475–479

    Abstract: The metaphase-to-anaphase transition is triggered by the Anaphase-Promoting Complex (APC), an E3 ubiquitin ligase that targets proteins for degradation, leading to sister chromatid separation and mitotic exit. The function of APC is controlled by the ... ...

    Abstract The metaphase-to-anaphase transition is triggered by the Anaphase-Promoting Complex (APC), an E3 ubiquitin ligase that targets proteins for degradation, leading to sister chromatid separation and mitotic exit. The function of APC is controlled by the spindle checkpoint that delays anaphase onset in the presence of any chromosome that has not established bipolar attachment to the mitotic spindle. In this way, the checkpoint ensures accurate chromosome segregation. The spindle checkpoint is mostly activated from kinetochores that are not attached to microtubules or not under tension that is normally generated from bipolar attachment. These kinetochores recruit several spindle checkpoint proteins to assemble an inhibitory complex composed of checkpoint proteins Mad2, Bub3, and Mad3/BubR1. This complex binds and inhibits Cdc20, an activator and substrate adaptor for APC. In addition, the checkpoint complex promotes Cdc20 degradation, thus lowering Cdc20 protein level upon checkpoint activation. This dual inhibition on Cdc20 likely ensures that the spindle checkpoint is sustained even when the cell contains only a single unattached kinetochore.
    MeSH term(s) Anaphase-Promoting Complex-Cyclosome ; Animals ; Cdc20 Proteins ; Cell Cycle Proteins/antagonists & inhibitors ; Cell Cycle Proteins/metabolism ; Genes, cdc ; Humans ; Models, Genetic ; Signal Transduction ; Spindle Apparatus/genetics ; Spindle Apparatus/metabolism ; Ubiquitin-Protein Ligase Complexes/metabolism
    Chemical Substances Cdc20 Proteins ; Cell Cycle Proteins ; CDC20 protein, human (156288-95-8) ; Ubiquitin-Protein Ligase Complexes (EC 2.3.2.23) ; Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27)
    Language English
    Publishing date 2007-07
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1193378-1
    ISSN 1423-0127 ; 1021-7770
    ISSN (online) 1423-0127
    ISSN 1021-7770
    DOI 10.1007/s11373-007-9157-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4037: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: Cdc48 chaperone and adaptor Ubx4 distribute the proteasome in the nucleus for anaphase proteolysis.

    Chien, Chen-Ying / Chen, Rey-Huei

    The Journal of biological chemistry

    2013  Volume 288, Issue 52, Page(s) 37180–37191

    Abstract: The cell cycle transition is driven by abrupt degradation of key regulators. While ubiquitylation of these proteins has been extensively studied, the requirement for the proteolytic step is less understood. By analyzing the cell cycle function of Cdc48 ... ...

    Abstract The cell cycle transition is driven by abrupt degradation of key regulators. While ubiquitylation of these proteins has been extensively studied, the requirement for the proteolytic step is less understood. By analyzing the cell cycle function of Cdc48 in the budding yeast Saccharomyces cerevisiae, we found that double mutations in Cdc48 and its adaptor Ubx4 cause mitotic arrest with sustained Clb2 and Cdc20 proteins that are normally degraded in anaphase. The phenotype is neither caused by spindle checkpoint activation nor a defect in the assembly or the activity of the ubiquitylation machinery and the proteasome. Interestingly, the 26S proteasome is mislocalized into foci, which are colocalized with nuclear envelope anchor Sts1 in cdc48-3 ubx4 cells. Moreover, genetic analysis reveals that ubx4 deletion mutant dies in the absence of Rpn4, a transcriptional activator for proteasome subunits, and the proteasome chaperone Ump1, indicating that an optimal level of the proteasome is required for survival. Overexpression of Rpn4 indeed can rescue cell growth and anaphase proteolysis in cdc48-3 ubx4 cells. Biochemical analysis further shows that Ubx4 interacts with the proteasome. Our data propose that Cdc48-Ubx4 acts on the proteasome and uses the chaperone activity to promote its nuclear distribution, thereby optimizing the proteasome level for efficient degradation of mitotic regulators.
    MeSH term(s) Active Transport, Cell Nucleus/physiology ; Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Anaphase/physiology ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Gene Deletion ; Intracellular Signaling Peptides and Proteins ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Spindle Apparatus/genetics ; Spindle Apparatus/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Valosin Containing Protein
    Chemical Substances Carrier Proteins ; Cell Cycle Proteins ; DNA-Binding Proteins ; Intracellular Signaling Peptides and Proteins ; Molecular Chaperones ; RPN4 protein, S cerevisiae ; STS1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Transcription Factors ; UBX4 protein, S cerevisiae ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; ATP dependent 26S protease (EC 3.4.99.-) ; Adenosine Triphosphatases (EC 3.6.1.-) ; CDC48 protein, S cerevisiae (EC 3.6.4.-) ; Valosin Containing Protein (EC 3.6.4.6)
    Language English
    Publishing date 2013-11-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M113.513598
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: Lipid droplets are central organelles for meiosis II progression during yeast sporulation.

    Hsu, Tzu-Han / Chen, Rey-Huei / Cheng, Yun-Hsin / Wang, Chao-Wen

    Molecular biology of the cell

    2017  Volume 28, Issue 3, Page(s) 440–451

    Abstract: Neutral lipids, predominantly triacylglycerol (TAG) and sterol ester, are stored within the cellular organelles termed lipid droplets (LDs). Although it is believed that the major function of LDs is to supply the cell with energy and membranes, little is ...

    Abstract Neutral lipids, predominantly triacylglycerol (TAG) and sterol ester, are stored within the cellular organelles termed lipid droplets (LDs). Although it is believed that the major function of LDs is to supply the cell with energy and membranes, little is known about the cellular events directly involving LDs and their contents. In this study, we provide cytological evidence that LDs form direct contacts with the prospore membrane (PSM) that is synthesized de novo during meiosis II to sequester the dividing nuclei in sporulating yeast. Lipidomic analyses indicate that TAG lipolysis releases free fatty acids at a time that correlates well with meiosis II progression, concomitant with phospholipid remodeling. Mutants lacking TAG or impaired of TAG hydrolysis show spore wall assembly defects, supporting a role for TAG and/or its metabolites in spore wall morphogenesis. Not only does LD integrity influence spore wall assembly, LDs are also essential for other aspects of spore development. Yeast cells lacking LDs are severely defective in PSM growth and organization and display disrupted spindles, producing dead spores or even failing to form spores. Together these results link LD physiology directly to a unique membrane morphogenesis process critical for development.
    MeSH term(s) Cell Membrane/physiology ; Cell Wall/metabolism ; Lipid Droplets/metabolism ; Lipid Droplets/physiology ; Lipid Metabolism/physiology ; Lipids/physiology ; Lipolysis/physiology ; Meiosis/physiology ; Organelles/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Spores, Fungal/metabolism
    Chemical Substances Lipids ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2017-02-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E16-06-0375
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: 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)
    Zs.MO 410: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article: Phosphorylation and activation of Bub1 on unattached chromosomes facilitate the spindle checkpoint.

    Chen, Rey-Huei

    The EMBO journal

    2004  Volume 23, Issue 15, Page(s) 3113–3121

    Abstract: The spindle checkpoint inhibits anaphase until all kinetochores have attached properly to spindle microtubules. The protein kinase Bub1 is an essential checkpoint component that resides at kinetochores during mitosis. It is shown herein that Xenopus Bub1 ...

    Abstract The spindle checkpoint inhibits anaphase until all kinetochores have attached properly to spindle microtubules. The protein kinase Bub1 is an essential checkpoint component that resides at kinetochores during mitosis. It is shown herein that Xenopus Bub1 becomes hyperphosphorylated and the kinase is activated on unattached chromosomes. MAP kinase (MAPK) contributes to this phosphorylation, as inhibiting MAPK or altering MAPK consensus sites in Bub1 to alanine or valine (Bub1(5AV)) abolishes the phosphorylation and activation on chromosomes. Both Bub1 and Bub1(5AV) support the checkpoint under an optimal condition for spindle checkpoint activation. However, Bub1, but not Bub1(5AV), supports the checkpoint at a relatively low concentration of nuclei or the microtubule inhibitor nocodazole. Similar to Bub1(5AV), Bub1 without the kinase domain (Bub1(deltaKD)) is also partially compromised in its checkpoint function and in its ability to recruit other checkpoint proteins to kinetochores. This study suggests that activation of Bub1 at kinetochores enhances the efficiency of the spindle checkpoint and is probably important in maintaining the checkpoint toward late prometaphase when the cell contains only a few or a single unattached kinetochore.
    MeSH term(s) Animals ; Cell Cycle ; Cell Cycle Proteins ; Chromosomes/metabolism ; Enzyme Activation ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Kinetochores/metabolism ; Mutation/genetics ; Ovum/cytology ; Ovum/metabolism ; Phosphorylation ; Protein Kinases/genetics ; Protein Kinases/metabolism ; Protein Serine-Threonine Kinases ; Spindle Apparatus/metabolism ; Xenopus laevis
    Chemical Substances Cell Cycle Proteins ; Protein Kinases (EC 2.7.-) ; Bub1 spindle checkpoint protein (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
    Language English
    Publishing date 2004-07-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/sj.emboj.7600308
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1808: 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)
    Zs.MG 100: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article ; Online: Cdc48 and cofactors Npl4-Ufd1 are important for G1 progression during heat stress by maintaining cell wall integrity in Saccharomyces cerevisiae.

    Hsieh, Meng-Ti / Chen, Rey-Huei

    PloS one

    2011  Volume 6, Issue 4, Page(s) e18988

    Abstract: The ubiquitin-selective chaperone Cdc48, a member of the AAA (ATPase Associated with various cellular Activities) ATPase superfamily, is involved in many processes, including endoplasmic reticulum-associated degradation (ERAD), ubiquitin- and proteasome- ... ...

    Abstract The ubiquitin-selective chaperone Cdc48, a member of the AAA (ATPase Associated with various cellular Activities) ATPase superfamily, is involved in many processes, including endoplasmic reticulum-associated degradation (ERAD), ubiquitin- and proteasome-mediated protein degradation, and mitosis. Although Cdc48 was originally isolated as a cell cycle mutant in the budding yeast Saccharomyces cerevisiae, its cell cycle functions have not been well appreciated. We found that temperature-sensitive cdc48-3 mutant is largely arrested at mitosis at 37°C, whereas the mutant is also delayed in G1 progression at 38.5°C. Reporter assays show that the promoter activity of G1 cyclin CLN1, but not CLN2, is reduced in cdc48-3 at 38.5°C. The cofactor npl4-1 and ufd1-2 mutants also exhibit G1 delay and reduced CLN1 promoter activity at 38.5°C, suggesting that Npl4-Ufd1 complex mediates the function of Cdc48 at G1. The G1 delay of cdc48-3 at 38.5°C is a consequence of cell wall defect that over-activates Mpk1, a MAPK family member important for cell wall integrity in response to stress conditions including heat shock. cdc48-3 is hypersensitive to cell wall perturbing agents and is synthetic-sick with mutations in the cell wall integrity signaling pathway. Our results suggest that the cell wall defect in cdc48-3 is exacerbated by heat shock, which sustains Mpk1 activity to block G1 progression. Thus, Cdc48-Npl4-Ufd1 is important for the maintenance of cell wall integrity in order for normal cell growth and division.
    MeSH term(s) Adenosine Triphosphatases/metabolism ; Cell Cycle Proteins/metabolism ; Cell Wall/metabolism ; Cyclins/metabolism ; Endoplasmic Reticulum/metabolism ; Enzyme Activation ; G1 Phase ; Heat-Shock Response ; Nucleocytoplasmic Transport Proteins/metabolism ; Osmolar Concentration ; Phosphorylation ; Promoter Regions, Genetic/genetics ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins/metabolism ; Stress, Physiological ; Temperature ; Valosin Containing Protein ; Vesicular Transport Proteins/metabolism
    Chemical Substances Cell Cycle Proteins ; Cyclins ; NPL4 protein, S cerevisiae ; Nucleocytoplasmic Transport Proteins ; Saccharomyces cerevisiae Proteins ; UFD1 protein, S cerevisiae ; Vesicular Transport Proteins ; Adenosine Triphosphatases (EC 3.6.1.-) ; CDC48 protein, S cerevisiae (EC 3.6.4.-) ; Valosin Containing Protein (EC 3.6.4.6)
    Language English
    Publishing date 2011-04-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0018988
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  10. Article ; Online: Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor.

    Tseng, Li-Chuan / Chen, Rey-Huei

    Molecular biology of the cell

    2011  Volume 22, Issue 18, Page(s) 3306–3317

    Abstract: The nuclear envelope of metazoans disassembles during mitosis and reforms in late anaphase after sister chromatids have well separated. The coordination of these mitotic events is important for genome stability, yet the temporal control of nuclear ... ...

    Abstract The nuclear envelope of metazoans disassembles during mitosis and reforms in late anaphase after sister chromatids have well separated. The coordination of these mitotic events is important for genome stability, yet the temporal control of nuclear envelope reassembly is unknown. Although the steps of nuclear formation have been extensively studied in vitro using the reconstitution system from egg extracts, the temporal control can only be studied in vivo. Here, we use time-lapse microscopy to investigate this process in living HeLa cells. We demonstrate that Cdk1 activity prevents premature nuclear envelope assembly and that phosphorylation of the inner nuclear membrane protein lamin B receptor (LBR) by Cdk1 contributes to the temporal control. We further identify a region in the nucleoplasmic domain of LBR that inhibits premature chromatin binding of the protein. We propose that this inhibitory effect is partly mediated by Cdk1 phosphorylation. Furthermore, we show that the reduced chromatin-binding ability of LBR together with Aurora B activity contributes to nuclear envelope breakdown. Our studies reveal for the first time a mechanism that controls the timing of nuclear envelope reassembly through modification of an integral nuclear membrane protein.
    MeSH term(s) Amino Acid Substitution ; Anaphase ; Aurora Kinase B ; Aurora Kinases ; Binding Sites ; CDC2 Protein Kinase/antagonists & inhibitors ; CDC2 Protein Kinase/metabolism ; Chromatin/metabolism ; Endoplasmic Reticulum/metabolism ; Green Fluorescent Proteins/metabolism ; HeLa Cells ; Humans ; Microscopy, Fluorescence ; Mitosis ; Mutagenesis, Site-Directed ; Nuclear Envelope/metabolism ; Phosphorylation ; Protein Binding ; Protein Phosphatase 1/metabolism ; Protein Phosphatase 2/metabolism ; Protein Serine-Threonine Kinases/metabolism ; Protein Structure, Tertiary ; Purines/pharmacology ; Receptors, Cytoplasmic and Nuclear/chemistry ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Fusion Proteins/metabolism ; Roscovitine ; Single-Cell Analysis ; Time-Lapse Imaging ; Lamin B Receptor
    Chemical Substances Chromatin ; Purines ; Receptors, Cytoplasmic and Nuclear ; Recombinant Fusion Proteins ; Roscovitine (0ES1C2KQ94) ; Green Fluorescent Proteins (147336-22-9) ; AURKB protein, human (EC 2.7.11.1) ; Aurora Kinase B (EC 2.7.11.1) ; Aurora Kinases (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; CDC2 Protein Kinase (EC 2.7.11.22) ; Protein Phosphatase 1 (EC 3.1.3.16) ; Protein Phosphatase 2 (EC 3.1.3.16)
    Language English
    Publishing date 2011-07-27
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E11-03-0199
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: 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)
    Zs.MO 410: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top