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Nuclear pore protein TPR associates with lamin B1 and affects nuclear lamina organization and nuclear pore distribution

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    0521614 - ÚMG 2020 RIV CH eng J - Journal Article
    Fišerová, Jindřiška - Maninová, Miloslava - Sieger, T. - Uhlířová, Jana - Šebestová, Lenka - Efenberková, Michaela - Čapek, Martin - Fišer, K. - Hozák, Pavel
    Nuclear pore protein TPR associates with lamin B1 and affects nuclear lamina organization and nuclear pore distribution.
    Cellular and Molecular Life Sciences. Roč. 76, č. 11 (2019), s. 2199-2216. ISSN 1420-682X. E-ISSN 1420-9071
    R&D Projects: GA ČR GJ15-08835Y; GA ČR(CZ) GA16-03346S; GA ČR GA16-03403S; GA ČR(CZ) GA17-09103S; GA ČR(CZ) GA18-19714S; GA MŠMT(CZ) ED1.1.00/02.0109; GA MŠMT(CZ) LM2015062; GA MŠMT LO1419
    Institutional support: RVO:68378050
    Keywords : Translocated promoter region * tpr * Lamina * Lamins * Nuclear pore complex * Super-resolution imaging * Image analysis * Nucleus
    OECD category: Cell biology
    Impact factor: 6.496, year: 2019
    Method of publishing: Limited access
    https://link.springer.com/article/10.1007/s00018-019-03037-0

    The organization of the nuclear periphery is crucial for many nuclear functions. Nuclear lamins form dense network at the nuclear periphery and play a substantial role in chromatin organization, transcription regulation and in organization of nuclear pore complexes (NPCs). Here, we show that TPR, the protein located preferentially within the nuclear baskets of NPCs, associates with lamin B1. The depletion of TPR affects the organization of lamin B1 but not lamin A/C within the nuclear lamina as shown by stimulated emission depletion microscopy. Finally, reduction of TPR affects the distribution of NPCs within the nuclear envelope and the effect can be reversed by simultaneous knock-down of lamin A/C or the overexpression of lamin B1. Our work suggests a novel role for the TPR at the nuclear periphery: the TPR contributes to the organization of the nuclear lamina and in cooperation with lamins guards the interphase assembly of nuclear pore complexes.
    Permanent Link: http://hdl.handle.net/11104/0306213

     
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