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

J. Fišerová, M. Maninová, T. Sieger, J. Uhlířová, L. Šebestová, M. Efenberková, M. Čapek, K. Fišer, P. Hozák,

. 2019 ; 76 (11) : 2199-2216. [pub] 20190214

Jazyk angličtina Země Švýcarsko

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc19027816

Grantová podpora
15-08835Y Grantová Agentura České Republiky
16-03403S Grantová Agentura České Republiky
17-09103S Grantová Agentura České Republiky
18-19714S Grantová Agentura České Republiky
930218 Grantová Agentura, Univerzita Karlova
RVO: 68378050 Institute of Molecular Genetics CAS, v.v.i.
L200521801 Akademie Věd České Republiky
LM2015062 Ministerstvo školství, Mládeže a Tělovýchovy
CZ.2.16/3.1.00/21547 OPPK
LO1419 NPU I
CZ.02.1.01/0.0/0.0/16_013/0001775 ERDF
CZ.1.05/1.1.00/02.0109 Institute of Molecular Genetics

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.

Citace poskytuje Crossref.org

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