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Browsing by Author "Lloyd, D."

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    Adaptive changes in yeast membranes: catabolite repression and oxygen.
    (Portland Press, 1984) Jenkins, R. O.; Cartledge, T. G.; Lloyd, D.
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    Changes in proteinase activities and subcellular distribution during inactivation of alcohol oxidase in Candida boidinii
    (Portland Press, 1986-08) Jenkins, R. O.; Hill, D. L.; Cartledge, T. G.; Lloyd, D.
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    Respiratory adaptation of anaerobically grown Saccharomyces uvarum: Changes in distribution of enzymes
    (SOC GENERAL MICROBIOLOGY, 1984-11) Jenkins, R. O.; Cartledge, T. G.; Lloyd, D.
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    Subcellular Fractionation of Candida boidinii after Growth on Glucose or Methanol.
    (SOC GENERAL MICROBIOLOGY, 1985) Jenkins, R. O.; Cartledge, T. G.; Lloyd, D.
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    Subcellular Fractionation of Candida stellatoidea after Growth with Glucose or n-Hexadecane
    (SOC GENERAL MICROBIOLOGY, 1983-02) Jenkins, R. O.; Cartledge, T. G.; Lloyd, D.
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    SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
    (American Society for Microbiology, 2006-04-28) Haque, F.; Lloyd, D.; Smallwood, Dawn T.; Dent, C.; Shanahan, C.M.; Fry, A.M.; Trembath, R.; Shackleton, S.
    Nuclear migration and positioning within cells are critical for many developmental processes and are governed by the cytoskeletal network. Although mechanisms of nuclear-cytoskeletal attachment are unclear, growing evidence links a novel family of nuclear envelope (NE) proteins that share a conserved C-terminal SUN (Sad1/UNC-84 homology) domain. Analysis of Caenorhabditis elegans mutants has implicated UNC-84 in actin-mediated nuclear positioning by regulating NE anchoring of a giant actin-binding protein, ANC-1. Here, we report the identification of SUN1 as a lamin A-binding protein in a yeast two-hybrid screen. We demonstrate that SUN1 is an integral membrane protein located at the inner nuclear membrane. While the N-terminal domain of SUN1 is responsible for detergent-resistant association with the nuclear lamina and lamin A binding, lamin A/C expression is not required for SUN1 NE localization. Furthermore, SUN1 does not interact with type B lamins, suggesting that NE localization is ensured by binding to an additional nuclear component(s), most likely chromatin. Importantly, we find that the luminal C-terminal domain of SUN1 interacts with the mammalian ANC-1 homologs nesprins 1 and 2 via their conserved KASH domain. Our data provide evidence of a physical nuclear-cytoskeletal connection that is likely to be a key mechanism in nuclear-cytoplasmic communication and regulation of nuclear position.
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