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  1. Article ; Online: Control at the cell center: the role of spindle poles in cytoskeletal organization and cell cycle regulation.

    Cuschieri, Lara / Nguyen, Thao / Vogel, Jackie

    Cell cycle (Georgetown, Tex.)

    2007  Volume 6, Issue 22, Page(s) 2788–2794

    Abstract: Microtubule organizing centres (MTOCs), which include fungal spindle pole bodies and centrosome in higher eukaryotes, are a structurally diverse group of organelles that share a conserved role in microtubule nucleation and spindle formation. However, ... ...

    Abstract Microtubule organizing centres (MTOCs), which include fungal spindle pole bodies and centrosome in higher eukaryotes, are a structurally diverse group of organelles that share a conserved role in microtubule nucleation and spindle formation. However, recent studies propose that the function of MTOC components extends far beyond these established roles. Numerous cell cycle regulators, checkpoint proteins and microtubule plus tip binding proteins localize to MTOCs during the cell cycle, suggesting that these organelles serve as cellular scaffolds. In addition, several MTOC components such as gamma-tubulin and its associating proteins have been directly implicated in the control of cell cycle progression, activation of checkpoint responses and the regulation of microtubule organization and dynamics. Collectively, these findings implicate MTOCs as cellular control centers that coordinate events at both microtubule minus ends and plus ends with the cell cycle. In this review, we discuss recent studies that support a role for MTOC components, in particular gamma-tubulin, in cell cycle progression, checkpoint response and the coordination of microtubule organization and dynamics.
    MeSH term(s) Animals ; Cell Cycle/physiology ; Centrioles/chemistry ; Centrioles/physiology ; Cytoskeleton/chemistry ; Cytoskeleton/physiology ; Humans ; Microtubules/chemistry ; Microtubules/physiology ; Spindle Apparatus/chemistry ; Spindle Apparatus/physiology
    Language English
    Publishing date 2007-08-27
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2146183-1
    ISSN 1551-4005 ; 1538-4101 ; 1554-8627
    ISSN (online) 1551-4005
    ISSN 1538-4101 ; 1554-8627
    DOI 10.4161/cc.6.22.4941
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5881: 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)

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  2. Article: Gamma-tubulin is required for proper recruitment and assembly of Kar9-Bim1 complexes in budding yeast.

    Cuschieri, Lara / Miller, Rita / Vogel, Jackie

    Molecular biology of the cell

    2006  Volume 17, Issue 10, Page(s) 4420–4434

    Abstract: Microtubule plus-end-interacting proteins (+TIPs) promote the dynamic interactions between the plus ends (+ends) of astral microtubules and cortical actin that are required for preanaphase spindle positioning. Paradoxically, +TIPs such as the EB1 ... ...

    Abstract Microtubule plus-end-interacting proteins (+TIPs) promote the dynamic interactions between the plus ends (+ends) of astral microtubules and cortical actin that are required for preanaphase spindle positioning. Paradoxically, +TIPs such as the EB1 orthologue Bim1 and Kar9 also associate with spindle pole bodies (SPBs), the centrosome equivalent in budding yeast. Here, we show that deletion of four C-terminal residues of the budding yeast gamma-tubulin Tub4 (tub4-delta dsyl) perturbs Bim1 and Kar9 localization to SPBs and Kar9-dependent spindle positioning. Surprisingly, we find Kar9 localizes to microtubule +ends in tub4-delta dsyl cells, but these microtubules fail to position the spindle when targeted to the bud. Using cofluorescence and coaffinity purification, we show Kar9 complexes in tub4-delta dsyl cells contain reduced levels of Bim1. Astral microtubule dynamics is suppressed in tub4-delta dsyl cells, but it are restored by deletion of Kar9. Moreover, Myo2- and F-actin-dependent dwelling of Kar9 in the bud is observed in tub4-delta dsyl cells, suggesting defective Kar9 complexes tether microtubule +ends to the cortex. Overproduction of Bim1, but not Kar9, restores Kar9-dependent spindle positioning in the tub4-delta dsyl mutant, reduces cortical dwelling, and promotes Bim1-Kar9 interactions. We propose that SPBs, via the tail of Tub4, promote the assembly of functional +TIP complexes before their deployment to microtubule +ends.
    MeSH term(s) Actins ; Cell Cycle Proteins/metabolism ; Cell Cycle Proteins/physiology ; Cells, Cultured ; Microtubule Proteins/metabolism ; Microtubule Proteins/physiology ; Microtubules/metabolism ; Myosin Heavy Chains/metabolism ; Myosin Type V/metabolism ; Nuclear Proteins/metabolism ; Nuclear Proteins/physiology ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Saccharomyces cerevisiae Proteins/physiology ; Saccharomycetales/metabolism ; Signal Transduction ; Spindle Apparatus/metabolism ; Spindle Apparatus/ultrastructure ; Tubulin/genetics ; Tubulin/physiology
    Chemical Substances Actins ; BIM1 protein, S cerevisiae ; Cell Cycle Proteins ; KAR9 protein, S cerevisiae ; MYO2 protein, S cerevisiae ; Microtubule Proteins ; Nuclear Proteins ; Saccharomyces cerevisiae Proteins ; TUB4 protein, S cerevisiae ; Tubulin ; Myosin Type V (EC 3.6.1.-) ; Myosin Heavy Chains (EC 3.6.4.1)
    Language English
    Publishing date 2006-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E06-03-0245
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    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

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  3. Article: Spc24 and Stu2 promote spindle integrity when DNA replication is stalled.

    Ma, Lina / McQueen, Jennifer / Cuschieri, Lara / Vogel, Jackie / Measday, Vivien

    Molecular biology of the cell

    2007  Volume 18, Issue 8, Page(s) 2805–2816

    Abstract: The kinetochore, a protein complex that links chromosomes to microtubules (MTs), is required to prevent spindle expansion during S phase in budding yeast, but the mechanism of how the kinetochore maintains integrity of the bipolar spindle before mitosis ... ...

    Abstract The kinetochore, a protein complex that links chromosomes to microtubules (MTs), is required to prevent spindle expansion during S phase in budding yeast, but the mechanism of how the kinetochore maintains integrity of the bipolar spindle before mitosis is not well understood. Here, we demonstrate that a mutation of Spc24, a component of the conserved Ndc80 kinetochore complex, causes lethality when cells are exposed to the DNA replication inhibitor hydroxyurea (HU) due to premature spindle expansion and segregation of incompletely replicated DNA. Overexpression of Stu1, a CLASP-related MT-associated protein or a truncated form of the XMAP215 orthologue Stu2 rescues spc24-9 HU lethality and prevents spindle expansion. Truncated Stu2 likely acts in a dominant-negative manner, because overexpression of full-length STU2 does not rescue spc24-9 HU lethality, and spindle expansion in spc24-9 HU-treated cells requires active Stu2. Stu1 and Stu2 localize to the kinetochore early in the cell cycle and Stu2 kinetochore localization depends on Spc24. We propose that mislocalization of Stu2 results in premature spindle expansion in S phase stalled spc24-9 mutants. Identifying factors that restrain spindle expansion upon inhibition of DNA replication is likely applicable to the mechanism by which spindle elongation is regulated during a normal cell cycle.
    MeSH term(s) Anaphase/drug effects ; Cell Polarity/drug effects ; Chromosomal Proteins, Non-Histone/metabolism ; DNA Replication/drug effects ; Genes, Fungal ; Hydroxyurea/pharmacology ; Kinetochores/drug effects ; Kinetochores/metabolism ; Microbial Viability/drug effects ; Microtubule-Associated Proteins/metabolism ; Mutation/genetics ; Nuclear Proteins/metabolism ; Protein Transport/drug effects ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/drug effects ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Spindle Apparatus/drug effects ; Spindle Apparatus/metabolism
    Chemical Substances Chromosomal Proteins, Non-Histone ; Microtubule-Associated Proteins ; NDC80 protein, S cerevisiae ; Nuclear Proteins ; STU2 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Spc24 protein, S cerevisiae ; Hydroxyurea (X6Q56QN5QC)
    Language English
    Publishing date 2007-08
    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.E06-09-0882
    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

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