Depletion of nucleophosmin leads to distortion of nucleolar and nuclear structures in HeLa cells

Amin, Mohammed Abdullahel; Matsunaga, Sachihiro; Uchiyama, Susumu et al.

Biochemical Journal, 2008, 415(3), 345-351

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Identifier to cite or link to this item: https://hdl.handle.net/11094/79045

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Title
Depletion of nucleophosmin leads to distortion of nucleolar and nuclear structures in HeLa cells
Creator
CreatorName
Amin, Mohammed Abdullahel
NRID
1000040323448 1000040323448
CreatorName
Matsunaga, Sachihiro
NRID
1000090335381 1000090335381
ORCID
0000-0002-5181-179X 0000-0002-5181-179X
researchmap permalink
read0090387 read0090387
Scopus Author ID
35429790100 35429790100
CreatorName
Uchiyama, Susumu
NRID
1000000311770 1000000311770
researchmap permalink
read0068600 read0068600
CreatorName
Fukui, Kiichi
Subject
HeLa cell
Nuclear structure
Nucleolar structure
Nucleophosmin (NPM)
RNA interference (RNAi)
Description
Mohammed Abdullahel Amin, Sachihiro Matsunaga, Susumu Uchiyama, Kiichi Fukui; Depletion of nucleophosmin leads to distortion of nucleolar and nuclear structures in HeLa cells. Biochem J 1 November 2008; 415 (3): 345–351. doi: https://doi.org/10.1042/BJ20081411.
Abstract
NPM (nucleophosmin; also known as B23) is an abundantly and ubiquitously expressed multifunctional nucleolar phosphoprotein, which is involved in numerous cellular processes, including ribosome biogenesis, protein chaperoning and centrosome duplication; however, the role of NPM in the cell cycle still remains unknown. In the present study, we show dynamic localization of NPM throughout the cell cycle of HeLa cells. Using a combination of RNAi (RNA interference) and three-dimensional microscopy we show that NPM is localized at the chromosome periphery during mitosis. We also demonstrate that depletion of NPM causes distortion of nucleolar structure as expected and leads to unexpected dramatic changes in nuclear morphology with multiple micronuclei formation. The defect in nuclear shape of NPM-depleted cells, which is clearly observed by live-cell imaging, is due to the distortion of cytoskeletal (α-tubulin and β-actin) structure, resulting from the defects in centrosomal microtubule nucleation. These results indicate that NPM is an essential protein not only for the formation of normal nucleolar structure, but also for the maintenance of regular nuclear shape in HeLa cells.
Publisher
Biochemical Society
Source Title
Biochemical Journal
Volume (Issue)
415(3)
Page
345-351
Date of Issued
2008-10-15
Language
English
Handle URL
https://hdl.handle.net/11094/79045
PISSN
02646021
eISSN
14708728
NCID
AA10649144
Relation.isIdenticalTo
DOI (Publisher Version)
https://doi.org/10.1042/BJ20081411
PMID
18729828
Access Rights
open access
CopyRight
© 2008 The Author(s). This article is licensed under a Creative Commons Attribution-NonCommercial 2.5 Generic License.
oaire:version
Version of Record
Category
学術雑誌論文 Journal Article