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Related Experiment Video

Updated: Jun 24, 2026

Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells
06:29

Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells

Published on: July 30, 2020

ICIS and Aurora B coregulate the microtubule depolymerase Kif2a.

Anne L Knowlton1, Valeriya V Vorozhko, Weijie Lan

  • 1Department of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.

Current Biology : CB
|March 31, 2009
PubMed
Summary

This study explores how the microtubule-depolymerizing kinesin Kif2a is regulated during cell division. It finds that ICIS, a protein known to activate another kinesin called MCAK, can also reactivate Kif2a after it has been inhibited by Aurora B kinase. When ICIS activity is blocked, cells form monopolar spindles, a defect that can be corrected by adding anti-Nuf2 antibodies. The research also reveals that ICIS has distinct regions that bind to Aurora B and its regulators, as well as to MCAK, Kif2a, and microtubules. These findings suggest that ICIS acts as a scaffold, helping to coordinate the activity of these proteins during spindle formation.

Keywords:
ICIS functionKif2a regulationAurora B signalingMitotic spindle dynamics

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Live Cell Imaging to Assess the Dynamics of Metaphase Timing and Cell Fate Following Mitotic Spindle Perturbations
07:14

Live Cell Imaging to Assess the Dynamics of Metaphase Timing and Cell Fate Following Mitotic Spindle Perturbations

Published on: September 20, 2019

Area of Science:

  • Cell division regulation in molecular biology
  • Kinesin function in mitotic spindle dynamics
  • Chromosomal passenger complex signaling in cancer research

Background:

Microtubule dynamics are essential for spindle formation during cell division. While kinesin-13 proteins like Kif2a and MCAK are known to depolymerize microtubules, their regulation remains unclear. Aurora B kinase inhibits these depolymerases by phosphorylation, but how this inhibition is reversed is unknown. Prior research has shown that Aurora B inhibition reduces spindle bipolarity, but the mechanisms restoring activity are not well characterized. This gap motivated investigations into how Kif2a activity is reactivated. No prior work had resolved the role of ICIS in this process. Understanding these regulatory interactions could clarify how spindle structure is maintained. The focus on ICIS adds a new layer to the known signaling pathways. This paper contributes a novel perspective on spindle regulation.

Purpose Of The Study:

This study aimed to determine how Kif2a activity is restored after Aurora B inhibition. The researchers focused on the role of ICIS in this process. They hypothesized that ICIS might reactivate Kif2a after Aurora B suppression. The motivation stemmed from observations that ICIS activates MCAK, a related depolymerase. The study sought to clarify whether ICIS also regulates Kif2a. They tested this by injecting antibodies that block ICIS function into cells. The purpose was to observe the effects on spindle formation. This approach allowed them to assess ICIS's role in spindle dynamics. The study's goal was to uncover a new regulatory mechanism in mitotic spindle control.

Main Methods:

The researchers used antibody injections to block ICIS activity in cells. They observed spindle morphology after these treatments. They also used anti-Nuf2 antibodies to test for rescue effects. A structure-function analysis of ICIS was conducted to identify binding regions. The N-terminal region of ICIS was tested for Aurora B and INCENP binding. The central region was tested for interactions with MCAK and Kif2a. Microtubule binding experiments were performed to confirm ICIS's scaffold role. These methods allowed the team to map functional domains of ICIS.

Main Results:

ICIS was found to reactivate Kif2a after Aurora B inhibition. Blocking ICIS activity led to monopolar spindle formation. This phenotype was rescued by anti-Nuf2 antibody coinjection. Structure-function analysis showed the N terminus of ICIS binds Aurora B and its regulators. The central region of ICIS binds MCAK, Kif2a, and microtubules. These findings suggest ICIS acts as a scaffold for these proteins. ICIS binding to Aurora B and its regulators indicates a regulatory role. The data support a model where ICIS and the CPC regulate Kif2a activity.

Conclusions:

The authors propose that ICIS and the CPC regulate Kif2a depolymerase activity. ICIS appears to reactivate Kif2a after Aurora B inhibition. The scaffold function of ICIS is supported by its binding to multiple proteins. The study suggests ICIS interacts with Aurora B and its regulators. The central region of ICIS binds MCAK, Kif2a, and microtubules. This binding pattern supports a regulatory role for ICIS in spindle dynamics. The findings suggest ICIS is essential for restoring Kif2a activity. The study provides a framework for understanding spindle regulation.

ICIS reactivates Kif2a after Aurora B inhibition, as shown by monopolar spindle formation when ICIS activity is blocked.

The N terminus of ICIS binds Aurora B, INCENP, and TD60, suggesting a regulatory role in CPC signaling.

The central region binds MCAK, Kif2a, and microtubules, supporting a scaffold function for ICIS.

Anti-Nuf2 antibodies rescued the monopolar spindle phenotype caused by blocking ICIS activity.

Aurora B phosphorylates Kif2a's neck region, inhibiting its depolymerase activity.

The data suggest ICIS and the CPC regulate Kif2a depolymerase activity during spindle formation.