4.5 Article

Nuclear pore dynamics during the cell cycle

Journal

CURRENT OPINION IN CELL BIOLOGY
Volume 24, Issue 4, Pages 453-459

Publisher

CURRENT BIOLOGY LTD
DOI: 10.1016/j.ceb.2012.06.004

Keywords

-

Categories

Funding

  1. RIKEN Special Funding for Basic Science (Cellular System and Lipid Dynamics), Extreme Photonics
  2. Japan Society for the Promotion of Science (JSPS)
  3. Council for Science and Technology Policy (CSTP)
  4. Grants-in-Aid for Scientific Research [24570223] Funding Source: KAKEN

Ask authors/readers for more resources

A nuclear pore complex (NPC) is a large protein assembly that mediates the nucleocytoplasmic exchange of molecules. During the cell cycle, NPCs assemble, disassemble, and dynamically change their distribution on assembled nuclear envelope (NE), whereas in post-mitosis, NPCs are extremely stable. Extensive studies on its components, structure, and building blocks allow the study of its assembly and disassembly at the molecular level. Depending on the location that the initial components of this structure are built (e.g. chromatin versus double lipid bilayers of the nuclear envelope), the regulation and the mechanism of the assembly differ. Moreover, cell cycle dynamics of NPC are linked with INM proteins, lamins, lipid membranes, and the cell cycle signal, which show that NPC dynamics are highly regulated processes.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

Article Cell Biology

ELYS regulates the localization of LBR by modulating its phosphorylation state

Yasuhiro Mimura, Masatoshi Takagi, Michaela Clever, Naoko Imamoto

JOURNAL OF CELL SCIENCE (2016)

Article Cell Biology

Hikeshi modulates the proteotoxic stress response in human cells: Implication for the importance of the nuclear function of HSP70s

Khondoker Md Zulfiker Rahman, Hiroshi Mamada, Masatoshi Takagi, Shingo Kose, Naoko Imamoto

GENES TO CELLS (2017)

Article Biology

Extensive cargo identification reveals distinct biological roles of the 12 importin pathways

Makoto Kimura, Yuriko Morinaka, Kenichiro Imai, Shingo Kose, Paul Horton, Naoko Imamoto

ELIFE (2017)

Review Cell Biology

Heat stress-induced nuclear transport mediated by Hikeshi confers nuclear function of Hsp70s

Naoko Imamoto

CURRENT OPINION IN CELL BIOLOGY (2018)

Article Cell Biology

Nuclear transport adapts to varying heat stress in a multistep mechanism

Yutaka Ogawa, Naoko Imamoto

JOURNAL OF CELL BIOLOGY (2018)

Review Biochemistry & Molecular Biology

Nucleocytoplasmic transport under stress conditions and its role in HSP70 chaperone systems

Shingo Kose, Naoko Imamoto

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS (2014)

Article Biophysics

Analytic 3D Imaging of Mammalian Nucleus at Nanoscale Using Coherent X-Rays and Optical Fluorescence Microscopy

Changyong Song, Masatoshi Takagi, Jaehyun Park, Rui Xu, Marcus Gallagher-Jones, Naoko Imamoto, Tetsuya Ishikawa

BIOPHYSICAL JOURNAL (2014)

Article Biochemistry & Molecular Biology

The Schizosaccharomyces pombe Hikeshi/Opi10 protein has similar biochemical functions to its human homolog but acts in different physiological contexts

Yuumi Oda, Makoto Kimura, Shingo Kose, Milo B. Fasken, Anita H. Corbett, Naoko Imamoto

FEBS LETTERS (2014)

Article Biochemistry & Molecular Biology

Identification of Cargo Proteins Specific for Importin-β with Importin-α Applying a Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC)-based in Vitro Transport System

Makoto Kimura, Nobuaki Okumura, Shingo Kose, Toshifumi Takao, Naoko Imamoto

JOURNAL OF BIOLOGICAL CHEMISTRY (2013)

Correction Biochemistry & Molecular Biology

RAP55, a cytoplasmic mRNP component, represses translation in Xenopus oocytes (vol 281, pg 40096, 2006)

Kimio J. Tanaka, Kenji Ogawa, Masatoshi Takagi, Naoko Imamoto, Ken Matsumoto, Masafumi Tsujimoto

JOURNAL OF BIOLOGICAL CHEMISTRY (2014)

Article Biochemistry & Molecular Biology

Ki67 Antigen Contributes to the Timely Accumulation of Protein Phosphatase 1γ on Anaphase Chromosomes

Masatoshi Takagi, Yuko Nishiyama, Atsuko Taguchi, Naoko Imamoto

JOURNAL OF BIOLOGICAL CHEMISTRY (2014)

Article Biology

Ki-67 is a PP1-interacting protein that organises the mitotic chromosome periphery

Daniel G. Booth, Masatoshi Takagi, Luis Sanchez-Pulido, Elizabeth Petfalski, Giulia Vargiu, Kumiko Samejima, Naoko Imamoto, Chris P. Ponting, David Tollervey, William C. Earnshaw, Paola Vagnarelli

ELIFE (2014)

Article Cell Biology

The intrinsically disordered N-terminal region of mouse DNA polymerase alpha mediates its interaction with POT1a/b at telomeres

Takeshi Mizuno, Kei Hirabayashi, Sae Miyazawa, Yurika Kobayashi, Kenta Shoji, Masakazu Kobayashi, Fumio Hanaoka, Naoko Imamoto, Hidetaka Torigoe

Summary: The study investigated the interaction between DNA polymerase alpha and two paralogs of mouse POT1 telomere-binding protein, revealing their roles in lagging strand synthesis. Experimental results showed that the POT1a/b-TPP1-TIN2 complex accumulated in the nucleus, interacted with DNA polymerase alpha, and participated in telomere synthesis.

GENES TO CELLS (2021)

Article Biology

Lack of Hikeshi activates HSF1 activity under normal conditions and disturbs the heat-shock response

Shingo Kose, Kenichiro Imai, Ai Watanabe, Akira Nakai, Yutaka Suzuki, Naoko Imamoto

Summary: Hikeshi mediates the nuclear import of HSP70 and regulates its nucleocytoplasmic distribution and functions. Nuclear HSP70 affects the transcriptional activity of HSF1 and nuclear proteostasis. Depletion of Hikeshi leads to reduced nuclear HSP70 levels and up-regulation of HSF1-regulated gene expression.

LIFE SCIENCE ALLIANCE (2022)

No Data Available