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  1. Article: Securin Regulates the Spatiotemporal Dynamics of Separase.

    Sorensen Turpin, Christopher G / Sloan, Dillon / LaForest, Marian / Klebanow, Lindsey Uehlein / Mitchell, Diana / Severson, Aaron F / Bembenek, Joshua N

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Separase is a key regulator of the metaphase to anaphase transition with multiple functions. Separase cleaves cohesin to allow chromosome segregation and localizes to vesicles to promote exocytosis in mid-anaphase. The anaphase promoting complex/ ... ...

    Abstract Separase is a key regulator of the metaphase to anaphase transition with multiple functions. Separase cleaves cohesin to allow chromosome segregation and localizes to vesicles to promote exocytosis in mid-anaphase. The anaphase promoting complex/cyclosome (APC/C) activates separase by ubiquitinating its inhibitory chaperone, securin, triggering its degradation. How this pathway controls the exocytic function of separase has not been investigated. During meiosis I, securin is degraded over several minutes, while separase rapidly relocalizes from kinetochore structures at the spindle and cortex to sites of action on chromosomes and vesicles at anaphase onset. The loss of cohesin coincides with the relocalization of separase to the chromosome midbivalent at anaphase onset. APC/C depletion prevents separase relocalization, while securin depletion causes precocious separase relocalization. Expression of non-degradable securin inhibits chromosome segregation, exocytosis, and separase localization to vesicles but not to the anaphase spindle. We conclude that APC/C mediated securin degradation controls separase localization. This spatiotemporal regulation will impact the effective local concentration of separase for more precise targeting of substrates in anaphase.
    Language English
    Publishing date 2023-12-19
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.12.12.571338
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: BUB-1 targets PP2A:B56 to regulate chromosome congression during meiosis I in

    Bel Borja, Laura / Soubigou, Flavie / Taylor, Samuel J P / Fraguas Bringas, Conchita / Budrewicz, Jacqueline / Lara-Gonzalez, Pablo / Sorensen Turpin, Christopher G / Bembenek, Joshua N / Cheerambathur, Dhanya K / Pelisch, Federico

    eLife

    2020  Volume 9

    Abstract: Protein Phosphatase 2A (PP2A) is a heterotrimer composed of scaffolding (A), catalytic (C), and regulatory (B) subunits. PP2A complexes with B56 subunits are targeted by Shugoshin and BUBR1 to protect centromeric cohesion and stabilise kinetochore- ... ...

    Abstract Protein Phosphatase 2A (PP2A) is a heterotrimer composed of scaffolding (A), catalytic (C), and regulatory (B) subunits. PP2A complexes with B56 subunits are targeted by Shugoshin and BUBR1 to protect centromeric cohesion and stabilise kinetochore-microtubule attachments in yeast and mouse meiosis. In
    MeSH term(s) Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/metabolism ; Caenorhabditis elegans Proteins/physiology ; Chromosome Segregation ; Chromosomes/physiology ; Meiosis/physiology ; Oocytes/metabolism ; Oocytes/physiology ; Protein Phosphatase 2/metabolism ; Protein Phosphatase 2/physiology ; Protein Serine-Threonine Kinases/metabolism ; Protein Serine-Threonine Kinases/physiology
    Chemical Substances Caenorhabditis elegans Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; bub-1 protein, C elegans (EC 2.7.11.1) ; Protein Phosphatase 2 (EC 3.1.3.16)
    Language English
    Publishing date 2020-12-23
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Video-Audio Media
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.65307
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Conserved role for Ataxin-2 in mediating endoplasmic reticulum dynamics.

    Del Castillo, Urko / Gnazzo, Megan M / Sorensen Turpin, Christopher G / Nguyen, Ken C Q / Semaya, Emily / Lam, Yuwan / de Cruz, Matthew A / Bembenek, Joshua N / Hall, David H / Riggs, Blake / Gelfand, Vladimir I / Skop, Ahna R

    Traffic (Copenhagen, Denmark)

    2019  Volume 20, Issue 6, Page(s) 436–447

    Abstract: Ataxin-2, a conserved RNA-binding protein, is implicated in the late-onset neurodegenerative disease Spinocerebellar ataxia type-2 (SCA2). SCA2 is characterized by shrunken dendritic arbors and torpedo-like axons within the Purkinje neurons of the ... ...

    Abstract Ataxin-2, a conserved RNA-binding protein, is implicated in the late-onset neurodegenerative disease Spinocerebellar ataxia type-2 (SCA2). SCA2 is characterized by shrunken dendritic arbors and torpedo-like axons within the Purkinje neurons of the cerebellum. Torpedo-like axons have been described to contain displaced endoplasmic reticulum (ER) in the periphery of the cell; however, the role of Ataxin-2 in mediating ER function in SCA2 is unclear. We utilized the Caenorhabditis elegans and Drosophila homologs of Ataxin-2 (ATX-2 and DAtx2, respectively) to determine the role of Ataxin-2 in ER function and dynamics in embryos and neurons. Loss of ATX-2 and DAtx2 resulted in collapse of the ER in dividing embryonic cells and germline, and ultrastructure analysis revealed unique spherical stacks of ER in mature oocytes and fragmented and truncated ER tubules in the embryo. ATX-2 and DAtx2 reside in puncta adjacent to the ER in both C. elegans and Drosophila embryos. Lastly, depletion of DAtx2 in cultured Drosophila neurons recapitulated the shrunken dendritic arbor phenotype of SCA2. ER morphology and dynamics were severely disrupted in these neurons. Taken together, we provide evidence that Ataxin-2 plays an evolutionary conserved role in ER dynamics and morphology in C. elegans and Drosophila embryos during development and in fly neurons, suggesting a possible SCA2 disease mechanism.
    MeSH term(s) Animals ; Ataxin-2/metabolism ; Axonal Transport ; Caenorhabditis elegans ; Cells, Cultured ; Drosophila melanogaster ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/ultrastructure ; Evolution, Molecular ; Neuronal Outgrowth ; Neurons/metabolism ; Neurons/ultrastructure
    Chemical Substances Ataxin-2
    Language English
    Publishing date 2019-05-08
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12647
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5634: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  4. Article ; Online: Aurora B functions at the apical surface after specialized cytokinesis during morphogenesis in

    Bai, Xiaofei / Melesse, Michael / Sorensen Turpin, Christopher G / Sloan, Dillon E / Chen, Chin-Yi / Wang, Wen-Cheng / Lee, Po-Yi / Simmons, James R / Nebenfuehr, Benjamin / Mitchell, Diana / Klebanow, Lindsey R / Mattson, Nicholas / Betzig, Eric / Chen, Bi-Chang / Cheerambathur, Dhanya / Bembenek, Joshua N

    Development (Cambridge, England)

    2020  Volume 147, Issue 1

    Abstract: Although cytokinesis has been intensely studied, the way it is executed during development is not well understood, despite a long-standing appreciation that various aspects of cytokinesis vary across cell and tissue types. To address this, we ... ...

    Abstract Although cytokinesis has been intensely studied, the way it is executed during development is not well understood, despite a long-standing appreciation that various aspects of cytokinesis vary across cell and tissue types. To address this, we investigated cytokinesis during the invariant
    MeSH term(s) Animals ; Aurora Kinase B/physiology ; Caenorhabditis elegans/cytology ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans/enzymology ; Caenorhabditis elegans Proteins/physiology ; Cell Polarity ; Cytokinesis/physiology ; Dendrites/physiology ; Embryo, Nonmammalian/cytology ; Epithelial Cells/physiology ; Intestines/embryology ; Morphogenesis ; Neurons/cytology ; Pharynx/embryology ; Surface Properties
    Chemical Substances Caenorhabditis elegans Proteins ; Aurora Kinase B (EC 2.7.11.1) ; air-2 protein, C elegans (EC 2.7.11.1)
    Language English
    Publishing date 2020-01-08
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 90607-4
    ISSN 1477-9129 ; 0950-1991
    ISSN (online) 1477-9129
    ISSN 0950-1991
    DOI 10.1242/dev.181099
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ub I Zs.183: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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    Zs.MG 91: Show issues

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