4.7 Article

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

Journal

CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 76, Issue 11, Pages 2199-2216

Publisher

SPRINGER BASEL AG
DOI: 10.1007/s00018-019-03037-0

Keywords

Translocated promoter region; TPR; Lamina; Lamins; Nuclear pore complex; Super-resolution imaging; Image analysis; Nucleus

Funding

  1. Grant Agency of the Czech Republic [15-08835Y, 16-03346S, 16-03403S, 17-09103S, 18-19714S]
  2. project BIOCEV-Biotechnology and Biomedicine Centre of the Academy of Sciences and Charles University [CZ.1.05/1.1.00/02.0109]
  3. European Regional Development Fund
  4. ASCR [L200521801]
  5. GAUK [930218]
  6. MEYS CR [LM2015062]
  7. OPPK [CZ.2.16/3.1.00/21547]
  8. ERDF [CZ.02.1.01/0.0/0.0/16_013/0001775]
  9. NPU I [LO1419]
  10. institutional support of long-term conceptual support of development of the scientific organization [RVO: 68378050]

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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.

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