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  • 1
    Online Resource
    Online Resource
    Uncoupling of the spindle-checkpoint and chromosome-congression functions of BubR1
    The Company of Biologists ; 2010
    In:  Journal of Cell Science Vol. 123, No. 1 ( 2010-01-01), p. 84-94
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 123, No. 1 ( 2010-01-01), p. 84-94
    Abstract: The BubR1 checkpoint protein performs multiple functions in mitosis. We have carried out a functional analysis of conserved motifs of human BubR1 (also known as BUB1B) and demonstrate that spindle assembly checkpoint (SAC) and chromosome attachment functions can be uncoupled from each other. Mutation of five proline-directed serine phosphorylation sites, identified in vivo by mass spectrometry, essentially abolishes attachment of chromosomes to the spindle but has no effect on SAC functionality. By contrast, mutation of the two conserved KEN boxes required for SAC function does not impact chromosome congression. Interestingly, the contribution of the two KEN-box motifs is not equal. Cdc20 associates with the N-terminal but not C-terminal KEN box, and mutation of the N-terminal KEN motif results in more severe acceleration of mitotic timing. Moreover, the two KEN motifs are not sufficient for maximal binding of Cdc20 and APC/C, which also requires sequences in the BubR1 C-terminus. Finally, mutation of the GLEBS motif causes loss of Bub3 interaction and mislocalization of BubR1 from the kinetochore; concomitantly, BubR1 phosphorylation as well as SAC activity and chromosome congression are impaired, indicating that the GLEBS motif is strictly required for both major functions of human BubR1.
    Type of Medium: Online Resource
    ISSN: 1477-9137 , 0021-9533
    URL: Article
    DOI: 10.1242/jcs.056507
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2010
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    Identification and functional expression of ctaA, a P-type ATPase gene involved in copper trafficking in Trametes versicolor
    Microbiology Society ; 2003
    In:  Microbiology Vol. 149, No. 8 ( 2003-08-01), p. 2039-2048
    Details
    In: Microbiology, Microbiology Society, Vol. 149, No. 8 ( 2003-08-01), p. 2039-2048
    Abstract: Here the identification and characterization of a gene encoding a copper-trafficking enzyme, ctaA ( c opper- t ransporting A TPase), from the basidiomycete Trametes versicolor are described. This P-type copper ATPase gene has two alleles, differing primarily in the length of the second, unusually long intron, and encodes a 983 aa protein with 40 % sequence identity to yeast Ccc2p. Overexpression of ctaA in yeast grown in the presence of copper led to a 15-fold increase in laccase yields, while overexpression of ctaA and tahA , a previously identified copper homeostasis gene of T . versicolor , was additive, leading to a 20-fold increase in laccase production. In T . versicolor , overexpression of ctaA and tahA led to an eightfold increase in laccase expression, and a cotransformant still expressed laccase at 3000 μM copper when hardly any laccase activity is detected in the wild-type strain. Apparently, at low to moderate levels of copper tahA and ctaA overexpression disturbs the normal hierarchy of copper distribution, resulting in more being directed to the Golgi, while with high copper amounts that normally switch on the copper detoxification processes, tahA and ctaA gene products seem to out-compete the metallothionein copper chaperones, meaning laccase is still supplied with copper. These results may lead to a better understanding of copper trafficking and the hierarchy of copper distribution in the cell, and possibly be useful for constructing laccase-overproducing strains for biotechnological purposes.
    Type of Medium: Online Resource
    ISSN: 1350-0872 , 1465-2080
    URL: Article
    DOI: 10.1099/mic.0.26177-0
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2003
    detail.hit.zdb_id: 2008736-6
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Tension-sensitive Plk1 phosphorylation on BubR1 regulates the stability of kinetochore–microtubule interactions
    Cold Spring Harbor Laboratory ; 2007
    In:  Genes & Development Vol. 21, No. 17 ( 2007-09-01), p. 2205-2219
    Details
    In: Genes & Development, Cold Spring Harbor Laboratory, Vol. 21, No. 17 ( 2007-09-01), p. 2205-2219
    Abstract: Mitotic phosphorylation of the spindle checkpoint component BubR1 is highly conserved throughout evolution. Here, we demonstrate that BubR1 is phosphorylated on the Cdk1 site T620, which triggers the recruitment of Plk1 and phosphorylation of BubR1 by Plk1 both in vitro and in vivo. Phosphorylation does not appear to be required for spindle checkpoint function but instead is important for the stability of kinetochore–microtubule (KT–MT) interactions, timely mitotic progression, and chromosome alignment onto the metaphase plate. By quantitative mass spectrometry, we identify S676 as a Plk1-specific phosphorylation site on BubR1. Furthermore, using a phospho-specific antibody, we show that this site is phosphorylated during prometaphase, but dephosphorylated at metaphase upon establishment of tension between sister chromatids. These findings describe the first in vivo verified phosphorylation site for human BubR1, identify Plk1 as the kinase responsible for causing the characteristic mitotic BubR1 upshift, and attribute a KT-specific function to the hyperphosphorylated form of BubR1 in the stabilization of KT–MT interactions.
    Type of Medium: Online Resource
    ISSN: 0890-9369 , 1549-5477
    URL: Article
    DOI: 10.1101/gad.436007
    RVK:
    WA 15000
    Language: English
    Publisher: Cold Spring Harbor Laboratory
    Publication Date: 2007
    detail.hit.zdb_id: 1467414-2
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    Mitotic control of kinetochore-associated dynein and spindle orientation by human Spindly
    Rockefeller University Press ; 2009
    In:  Journal of Cell Biology Vol. 185, No. 5 ( 2009-06-01), p. 859-874
    Details
    In: Journal of Cell Biology, Rockefeller University Press, Vol. 185, No. 5 ( 2009-06-01), p. 859-874
    Abstract: Mitotic spindle formation and chromosome segregation depend critically on kinetochore–microtubule (KT–MT) interactions. A new protein, termed Spindly in Drosophila and SPDL-1 in C. elegans, was recently shown to regulate KT localization of dynein, but depletion phenotypes revealed striking differences, suggesting evolutionarily diverse roles of mitotic dynein. By characterizing the function of Spindly in human cells, we identify specific functions for KT dynein. We show that localization of human Spindly (hSpindly) to KTs is controlled by the Rod/Zw10/Zwilch (RZZ) complex and Aurora B. hSpindly depletion results in reduced inter-KT tension, unstable KT fibers, an extensive prometaphase delay, and severe chromosome misalignment. Moreover, depletion of hSpindly induces a striking spindle rotation, which can be rescued by co-depletion of dynein. However, in contrast to Drosophila, hSpindly depletion does not abolish the removal of MAD2 and ZW10 from KTs. Collectively, our data reveal hSpindly-mediated dynein functions and highlight a critical role of KT dynein in spindle orientation.
    Type of Medium: Online Resource
    ISSN: 1540-8140 , 0021-9525
    URL: Article
    URL: Article
    DOI: 10.1083/jcb.200812167
    DOI: 10.1083/jcb.200812167.dv
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2009
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis
    Rockefeller University Press ; 2005
    In:  The Journal of Cell Biology Vol. 171, No. 3 ( 2005-11-07), p. 431-436
    Details
    In: The Journal of Cell Biology, Rockefeller University Press, Vol. 171, No. 3 ( 2005-11-07), p. 431-436
    Abstract: Several kinases phosphorylate vimentin, the most common intermediate filament protein, in mitosis. Aurora-B and Rho-kinase regulate vimentin filament separation through the cleavage furrow-specific vimentin phosphorylation. Cdk1 also phosphorylates vimentin from prometaphase to metaphase, but its significance has remained unknown. Here we demonstrated a direct interaction between Plk1 and vimentin-Ser55 phosphorylated by Cdk1, an event that led to Plk1 activation and further vimentin phosphorylation. Plk1 phosphorylated vimentin at ∼1 mol phosphate/mol substrate, which partly inhibited its filament forming ability, in vitro. Plk1 induced the phosphorylation of vimentin-Ser82, which was elevated from metaphase and maintained until the end of mitosis. This elevation followed the Cdk1-induced vimentin-Ser55 phosphorylation, and was impaired by Plk1 depletion. Mutational analyses revealed that Plk1-induced vimentin-Ser82 phosphorylation plays an important role in vimentin filaments segregation, coordinately with Rho-kinase and Aurora-B. Taken together, these results indicated a novel mechanism that Cdk1 regulated mitotic vimentin phosphorylation via not only a direct enzyme reaction but also Plk1 recruitment to vimentin.
    Type of Medium: Online Resource
    ISSN: 1540-8140 , 0021-9525
    URL: Article
    DOI: 10.1083/jcb.200504091
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2005
    detail.hit.zdb_id: 1421310-2
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  • 6
    Online Resource
    Online Resource
    Plk4 trans -autophosphorylation regulates centriole number by controlling βTrCP-mediated degradation
    The Company of Biologists ; 2010
    In:  Journal of Cell Science Vol. 123, No. 13 ( 2010-07-01), p. 2163-2169
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 123, No. 13 ( 2010-07-01), p. 2163-2169
    Abstract: Centrioles are the main constituents of the mammalian centrosome and act as basal bodies for ciliogenesis. Centrosomes organize the cytoplasmic microtubule network during interphase and the mitotic spindle during mitosis, and aberrations in centrosome number have been implicated in chromosomal instability and tumor formation. The centriolar protein Polo-like kinase 4 (Plk4) is a key regulator of centriole biogenesis and is crucial for maintaining constant centriole number, but the mechanisms regulating its activity and expression are only beginning to emerge. Here, we show that human Plk4 is subject to βTrCP-dependent proteasomal degradation, indicating that this pathway is conserved from Drosophila to human. Unexpectedly, we found that stable overexpression of kinase-dead Plk4 leads to centriole overduplication. This phenotype depends on the presence of endogenous wild-type Plk4. Our data indicate that centriole overduplication results from disruption of Plk4 trans-autophosphorylation by kinase-dead Plk4, which then shields endogenous Plk4 from recognition by βTrCP. We conclude that active Plk4 promotes its own degradation by catalyzing βTrCP binding through trans-autophosphorylation (phosphorylation by the other kinase in the dimer) within homodimers.
    Type of Medium: Online Resource
    ISSN: 1477-9137 , 0021-9533
    URL: Article
    DOI: 10.1242/jcs.068502
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2010
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Identification and functional expression of tahA, a filamentous fungal gene involved in copper trafficking to the secretory pathway in Trametes versicolor
    Microbiology Society ; 2002
    In:  Microbiology Vol. 148, No. 12 ( 2002-12-01), p. 4049-4058
    Details
    In: Microbiology, Microbiology Society, Vol. 148, No. 12 ( 2002-12-01), p. 4049-4058
    Type of Medium: Online Resource
    ISSN: 1350-0872 , 1465-2080
    URL: Article
    DOI: 10.1099/00221287-148-12-4049
    Language: English
    Publisher: Microbiology Society
    Publication Date: 2002
    detail.hit.zdb_id: 2008736-6
    SSG: 12
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