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  • 1.
    Daigle, N
    et al.
    European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
    Beaudouin, J
    European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
    Hartnell, L
    NIH Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD), National Institutes of Health (NIH) - USA.
    Imreh, Gabriela
    Södertörns högskola, Avdelning Naturvetenskap.
    Hallberg, Einar
    Södertörns högskola, Avdelning Naturvetenskap.
    Lippincott-Schwartz, J
    NIH Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD), National Institutes of Health (NIH) - USA.
    Ellenberg, J
    European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
    Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells2001Inngår i: Journal of Cell Biology, ISSN 0021-9525, E-ISSN 1540-8140, Vol. 154, nr 1, s. 71-84Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    The nuclear pore complex (NPC) and its relationship to the nuclear envelope (NE) was characterized in living cells using POM121-green fluorescent protein (GFP) and GFP-Nup153, and GFP-lamin B1. No independent movement of single pore complexes was found within the plane of the NE in interphase. Only large arrays of NPCs moved slowly and synchronously during global changes in nuclear shape, strongly suggesting mechanical connections which form an NPC network. The nuclear lamina exhibited identical movements. NPC turnover measured by fluorescence recovery after photobleaching of POM121 was less than once per cell cycle. Nup153 association with NPCs was dynamic and turnover of this nucleoporin was three orders of magnitude faster. Overexpression of both nucleoporins induced the formation of annulate lamellae (AL) in the endoplasmic reticulum (ER). Turnover of AL pore complexes was much higher than in the NE (once every 2.5 min). During mitosis, POM121 and Nup153 were completely dispersed and mobile in the ER (POM121) or cytosol (Nup153) in metaphase, and rapidly redistributed to an immobilized pool around chromatin in late anaphase. Assembly and immobilization of both nucleoporins occurred before detectable recruitment of lamin B1, which is thus unlikely to mediate initiation of NPC assembly at the end of mitosis.

  • 2. Facanha, A L O
    et al.
    Appelgren, Henrik
    Södertörns högskola, Avdelning Naturvetenskap. Karolinska Institutet.
    Tabish, Mohammad
    Södertörns högskola, Avdelning Naturvetenskap. Karolinska Institutet.
    Okorokov, L
    Ekwall, Karl
    Södertörns högskola, Avdelning Naturvetenskap. Karolinska Institutet.
    The endoplasmic reticulum cation P-type ATPase Cta4p is required for control of cell shape and microtubule dynamics2002Inngår i: Journal of Cell Biology, ISSN 0021-9525, E-ISSN 1540-8140, Vol. 157, nr 6, s. 1029-1039Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Here we describe the phenotypic characterization of the cta(4+) gene, encoding a novel member of the P4 family of P-type ATPases of fission yeast. The cta4Delta mutant is temperature sensitive and cold sensitive lethal and displays several morphological defects in cell polarity and cytokinesis. Microtubules are generally destabilized in cells lacking Cta4p. The microtubule length is decreased, and the number of microtubules per cell is increased. This is concomitant with an increase in the number of microtubule catastrophe events in the midzone of the cell. These defects are likely due to a general imbalance in cation homeostasis. Immunofluorescence microscopy and membrane fractionation experiments revealed that green fluorescent protein-tagged Cta4 localizes to the ER. Fluorescence resonance energy transfer experiments in living cells using the yellow cameleon indicator for Ca2+ indicated that Cta4p regulates the cellular Ca2+ concentration. Thus, our results reveal a link between cation homeostasis and the control of cell shape, microtubule dynamics, and cytokinesis, and appoint Ca2+ as a key ion in controlling these processes.

  • 3. Zhang, H Q
    et al.
    Li, Z L
    Viklund, E K
    Strömblad, Staffan
    Södertörns högskola, Avdelning Naturvetenskap.
    P21-activated kinase 4 interacts with integrin alpha v beta 5 and regulates alpha v beta 5-mediated cell migration2002Inngår i: Journal of Cell Biology, ISSN 0021-9525, E-ISSN 1540-8140, Vol. 158, nr 7, s. 1287-1297Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    P21-activated kinase 1 (PAK1) can affect cell migration (Price et al., 1998; del Pozo et al., 2000) and modulate myosin light chain kinase and LIM kinase, which are components of the cellular motility machinery (Edwards, D.C., L.C. Sanders, G.M. Bokoch, and G.N. Gill. 1999. Nature Cell Biol. 1:253-259; Sanders, L.C., F. Matsumura, G.M. Bokoch, and P. de Lanerolle. 1999. Science. 283: 2083-2085). We here present a novel cell motility pathway by demonstrating that PAK4 directly interacts with an integrin intracellular domain and regulates carcinoma cell motility in an integrin-specific manner. Yeast two-hybrid screening identified PAK4 binding to the cytoplasmic domain of the integrin beta5 subunit, an association that was also found in mammalian cells between endogenous PAK4 and integrin alphavbeta5. Furthermore, we mapped the PAK4 binding to the membrane-proximal region of integrin beta5, and identified an integrin-binding domain at aa 505-530 in the COOH terminus of PAK4. Importantly, engagement of integrin alphavbeta5 by cell attachment to vitronectin led to a redistribution of PAK4 from the cytosol to dynamic lamellipodial structures where PAK4 colocalized with integrin alphavbeta5. Functionally, PAK4 induced integrin alphavbeta5-mediated, but not beta1-mediated, human breast carcinoma cell migration, while no changes in integrin cell surface expression levels were observed. In conclusion, our results demonstrate that PAK4 interacts with integrin alphavbeta5 and selectively promotes integrin alphavbeta5-mediated cell migration.

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