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

• Published in: Cellular and molecular life sciences : CMLS Vol. 76; no. 11; pp. 2199 - 2216
• Main Authors: Fišerová, Jindřiška, Maninová, Miloslava, Sieger, Tomáš, Uhlířová, Jana, Šebestová, Lenka, Efenberková, Michaela, Čapek, Martin, Fišer, Karel, Hozák, Pavel
• Format: Journal Article
• Language: English
• Published: Cham Springer International Publishing 01-06-2019; Springer Nature B.V
• Subjects: Baskets; Biochemistry; Biomedical and Life Sciences; Biomedicine; Cell Biology; Chromatin; Depletion; Emissions control; Gene Expression Regulation; Gene regulation; Guards; HeLa Cells; Humans; Lamin Type A - antagonists & inhibitors; Lamin Type A - genetics; Lamin Type A - metabolism; Lamin Type B - genetics; Lamin Type B - metabolism; Lamins; Life Sciences; Molecular Imaging; Nuclear Envelope - metabolism; Nuclear Envelope - ultrastructure; Nuclear Lamina - metabolism; Nuclear Lamina - ultrastructure; Nuclear Pore Complex Proteins - antagonists & inhibitors; Nuclear Pore Complex Proteins - genetics; Nuclear Pore Complex Proteins - metabolism; Original; Original Article; Proteins; Proto-Oncogene Proteins - antagonists & inhibitors; Proto-Oncogene Proteins - genetics; Proto-Oncogene Proteins - metabolism; RNA, Small Interfering - genetics; RNA, Small Interfering - metabolism; Signal Transduction; Stimulated emission; Transcription; Nucleus; Image analysis; Nuclear pore complex; TPR; Lamins; Super-resolution imaging; Translocated promoter region; Lamina
• ISSN: 1420-682X; 1420-9071
• DOI: 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.