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Related Concept Videos

The Contractile Ring02:15

The Contractile Ring

Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
The Contractile Ring02:15

The Contractile Ring

Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...

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Related Experiment Video

Updated: Jun 3, 2026

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast
11:19

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast

Published on: February 20, 2017

Importin-β1 functions as a chromatin sensor to position the contractile ring for cytokinesis.

Cecilia Rachelle Brancheriau1, Kevin Larocque1, Gabrielle Schick1

  • 1Biology Department, Concordia University, Montréal, QC H4B 1R6, Canada.

Current Biology : CB
|June 1, 2026
PubMed
Summary

Importins form a gradient during cell division, crucial for positioning the actomyosin ring in cancer cells. This importin-mediated anillin recruitment offers a potential therapeutic target in aneuploid cancer cells.

Keywords:
Ran-gradientaneuploidyanillinchromatincytokinesisimportin-β1mitosismodeling

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Last Updated: Jun 3, 2026

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast
11:19

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast

Published on: February 20, 2017

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
11:50

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Cytokinesis requires precise actomyosin ring positioning, regulated by chromatin-associated Ran-GTP.
  • The precise mechanism by which Ran-GTP influences ring positioning, particularly involving importins, remains unclear.
  • Importins are key nuclear transport proteins, but their role during anaphase and cytokinesis is not well understood.

Purpose of the Study:

  • To investigate whether importins form a gradient in response to chromatin-associated Ran-GTP during cell division.
  • To determine if importins regulate actomyosin ring assembly and ingression.
  • To explore the potential of importin-mediated pathways as a therapeutic target in aneuploid cancer cells.

Main Methods:

  • Endogenous tagging of importin-β1 with mNeonGreen in HeLa and HCT 116 cell lines.
  • Live-cell imaging to observe importin-β1 localization during anaphase.
  • Optogenetic tools to rapidly disrupt importin-β1 function and FLIM-FRET imaging to assess Ran-binding status.

Main Results:

  • Importin-β1 transiently enriched between segregating chromosomes in anaphase HeLa cells, but not HCT 116 cells.
  • Disruption of importin-β1 function impaired actomyosin ring ingression in HeLa cells, indicating its requirement.
  • Ran-free importin-β1 enrichment at the equator was observed in HeLa cells, dependent on the chromatin-to-cytosol ratio.

Conclusions:

  • Importin-β1 forms a Ran-GTP-dependent gradient that is crucial for actomyosin ring positioning in certain cell types.
  • The chromatin-to-cytosol ratio significantly influences importin-β1 and anillin localization, impacting ring assembly.
  • Aneuploid cancer cells' reliance on importin-mediated anillin recruitment presents a potential targetable vulnerability.