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  1. Article: Orchestrating the cell cycle in yeast: sequential localization of key mitotic regulators at the spindle pole and the bud neck.

    Cid, Vı Ctor J / Jiménez, Javier / Molina, Marı A / Sánchez, Miguel / Nombela, César / Thorner, Jeremy W

    Microbiology (Reading, England)

    2001  Volume 148, Issue Pt 9, Page(s) 2647–2659

    MeSH term(s) CDC28 Protein Kinase, S cerevisiae/metabolism ; Cell Cycle Proteins ; Gene Expression Regulation, Fungal ; Mitosis/physiology ; Morphogenesis ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins
    Chemical Substances Cell Cycle Proteins ; Saccharomyces cerevisiae Proteins ; Protein Kinases (EC 2.7.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; CDC5 protein, S cerevisiae (EC 2.7.11.21) ; CDC28 Protein Kinase, S cerevisiae (EC 2.7.11.22)
    Language English
    Publishing date 2001-08-13
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 1180712-x
    ISSN 1465-2080 ; 1350-0872
    ISSN (online) 1465-2080
    ISSN 1350-0872
    DOI 10.1099/00221287-148-9-2647
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article: Cell cycle control of septin ring dynamics in the budding yeast.

    Cid, Vı Ctor J / Adamiková, Lubica / Sánchez, Miguel / Molina, Marı A / Nombela, César

    Microbiology (Reading, England)

    2001  Volume 147, Issue Pt 6, Page(s) 1437–1450

    Abstract: Septins constitute a cytoskeletal structure that is conserved in eukaryotes. In Saccharomyces cerevisiae, the Cdc3, Cdc10, Cdc11, Cdc12 and Shs1/Sep7 septins assemble as a ring that marks the cytokinetic plane throughout the budding cycle. This structure ...

    Abstract Septins constitute a cytoskeletal structure that is conserved in eukaryotes. In Saccharomyces cerevisiae, the Cdc3, Cdc10, Cdc11, Cdc12 and Shs1/Sep7 septins assemble as a ring that marks the cytokinetic plane throughout the budding cycle. This structure participates in different aspects of morphogenesis, such as selection of cell polarity, localization of chitin synthesis, the switch from hyperpolar to isotropic bud growth after bud emergence and the spatial regulation of septation. The septin cytoskeleton assembles at the pre-bud site before bud emergence, remains there during bud growth and duplicates at late mitosis eventually disappearing after cell separation. Using a septin-GFP fusion and time-lapse confocal microscopy, we have determined that septin dynamics are maintained in budding zygotes and during unipolar synchronous growth in pseudohyphae. By means of specific cell cycle arrests and deregulation of cell cycle controls we show that septin assembly is dependent on G1 cyclin/Cdc28-mediated cell cycle signals and that the small GTPase Cdc42, but not Rho1, are essential for this event. However, during bud growth, the septin ring shapes a bud-neck-spanning structure that is unaffected by failures in the regulation of mitosis, such as activation of the DNA repair or spindle assembly checkpoints or inactivation of the anaphase-promoting complex (APC). At the end of the cell cycle, the splitting of the ring into two independent structures depends on the function of the mitotic exit network in which the protein phosphatase Cdc14 participates. Our data support a role of cell cycle control mechanisms in the regulation of septin dynamics to accurately coordinate morphogenesis throughout the budding process in yeast.
    MeSH term(s) Anaphase-Promoting Complex-Cyclosome ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; GTP Phosphohydrolases ; Gene Expression Regulation, Fungal ; Green Fluorescent Proteins ; Ligases/genetics ; Ligases/metabolism ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Membrane Proteins ; Microscopy, Confocal ; Mitosis ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces pombe Proteins ; Signal Transduction ; Transcription Factors ; Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; cdc42 GTP-Binding Protein, Saccharomyces cerevisiae/genetics ; cdc42 GTP-Binding Protein, Saccharomyces cerevisiae/metabolism ; rho GTP-Binding Proteins/genetics ; rho GTP-Binding Proteins/metabolism
    Chemical Substances Cell Cycle Proteins ; Cytoskeletal Proteins ; Luminescent Proteins ; Membrane Proteins ; Recombinant Fusion Proteins ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces pombe Proteins ; Transcription Factors ; cdc10 protein, S pombe ; Green Fluorescent Proteins (147336-22-9) ; Ubiquitin-Protein Ligase Complexes (EC 2.3.2.23) ; Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; CDC10 protein, S cerevisiae (EC 3.6.1.-) ; GTP Phosphohydrolases (EC 3.6.1.-) ; RHO1 protein, S cerevisiae (EC 3.6.5.2) ; cdc42 GTP-Binding Protein, Saccharomyces cerevisiae (EC 3.6.5.2) ; rho GTP-Binding Proteins (EC 3.6.5.2) ; Ligases (EC 6.-)
    Language English
    Publishing date 2001-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1180712-x
    ISSN 1465-2080 ; 1350-0872
    ISSN (online) 1465-2080
    ISSN 1350-0872
    DOI 10.1099/00221287-147-6-1437
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.140: Show issues Location:
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