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Updated: May 31, 2026

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles
Published on: May 10, 2022
Kif18B interacts with EB1 and controls astral microtubule length during mitosis
Jane R Stout1, Amber L Yount, James A Powers
1Medical Sciences Program, Indiana University, Bloomington, IN 47405, USA.
Abstract:
Regulation of microtubule (MT) dynamics is essential for proper spindle assembly and organization. Kinesin-8 family members are plus-end-directed motors that modulate plus-end MT dynamics by acting as MT depolymerases or as MT plus-end capping proteins. In this paper, we show that the human kinesin-8 Kif18B functions during mitosis to control astral MT organization. Kif18B is a MT plus-tip-tracking protein that localizes to the nucleus in interphase and is enriched at astral MT plus ends during early mitosis. Knockdown of Kif18B caused spindle defects, resulting in an increased number and length of MTs. A yeast two-hybrid screen identified an interaction of the C-terminal domain of Kif18B with the plus-end MT-binding protein EB1. EB1 knockdown disrupted Kif18B targeting to MT plus ends, indicating that EB1/Kif18B interaction is physiologically important. This interaction is direct, as the far C-terminal end of Kif18B is sufficient for binding to EB1 in vitro. Overexpression of this domain is sufficient for plus-end MT targeting in cells; however, targeting is enhanced by the motor domain, which cooperates with the tail to achieve proper Kif18B localization at MT plus ends. Our results suggest that Kif18B is a new MT dynamics regulatory protein that interacts with EB1 to control astral MT length.
Insights
Human kinesin-8 Kif18B regulates astral microtubule (MT) organization during mitosis. It interacts with EB1 to control MT length, impacting spindle assembly.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Microtubule (MT) dynamics are crucial for cell division, particularly spindle assembly.
- Kinesin-8 motors regulate MT dynamics, acting as depolymerases or capping proteins at MT plus ends.
Purpose of the Study:
- To investigate the role of human kinesin-8 Kif18B in mitotic astral MT organization.
- To identify proteins interacting with Kif18B and elucidate its mechanism of action.
Main Methods:
- Kif18B knockdown experiments to observe effects on MTs and spindle.
- Yeast two-hybrid screening to identify interacting proteins.
- In vitro binding assays and cell-based overexpression studies.
Main Results:
- Kif18B knockdown led to increased MT number and length, causing spindle defects.
- Kif18B directly interacts with the MT plus-end-binding protein EB1.
- EB1 is necessary for Kif18B's proper localization to MT plus ends.
Conclusions:
- Kif18B is a novel MT plus-tip-tracking protein that regulates astral MT length during mitosis.
- The interaction between Kif18B and EB1 is critical for Kif18B's function and localization.
- Kif18B, in conjunction with EB1, plays a key role in controlling MT dynamics for proper spindle organization.
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