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Updated: May 3, 2026

Using plusTipTracker Software to Measure Microtubule Dynamics in Xenopus laevis Growth Cones
Published on: September 7, 2014
Mcp1p tracks microtubule plus ends to destabilize microtubules at cell tips
Fan Zheng1, Tianpeng Li1, Martin Cheung2
1HKU-Shenzhen Institute of Research and Innovation, The University of Hong Kong, Shenzhen, China; Department of Biochemistry, The University of Hong Kong, Pokfulam, Hong Kong, China.
Abstract:
Microtubule plus ends are dynamically regulated by a wide variety of proteins for performing diverse cellular functions. Here, we show that the fission yeast Schizosaccharomyces pombe uncharacterized protein mcp1p is a microtubule plus-end tracking protein which depends on the kinesin-8 klp6p for transporting along microtubules towards microtubule plus ends. In the absence of mcp1p, microtubule catastrophe and rescue frequencies decrease, leading to an increased dwell time of microtubule plus ends at cell tips. Thus, these findings suggest that mcp1p may synergize with klp6p at microtubule plus-ends to destabilize microtubules.
Insights
The fission yeast protein mcp1p tracks microtubule plus ends, requiring kinesin-8 klp6p. Without mcp1p, microtubules become more stable, suggesting mcp1p and klp6p destabilize microtubule plus ends.
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- Microtubule dynamics are crucial for cellular functions.
- Microtubule plus-end tracking proteins regulate microtubule behavior.
- The fission yeast Schizosaccharomyces pombe is a model organism for studying cell division and dynamics.
Purpose of the Study:
- To characterize the function of the uncharacterized protein mcp1p in fission yeast.
- To investigate the role of mcp1p in microtubule dynamics.
- To determine the relationship between mcp1p and the kinesin-8 klp6p.
Main Methods:
- Utilized Schizosaccharomyces pombe as a model organism.
- Investigated microtubule plus-end tracking behavior of mcp1p.
- Assessed the dependence of mcp1p transport on klp6p.
- Analyzed microtubule catastrophe and rescue frequencies in the absence of mcp1p.
Main Results:
- Identified mcp1p as a microtubule plus-end tracking protein.
- Demonstrated that mcp1p transport depends on the kinesin-8 klp6p.
- Observed decreased microtubule catastrophe and rescue frequencies in mcp1p-deficient cells.
- Found an increased dwell time of microtubule plus ends at cell tips in the absence of mcp1p.
Conclusions:
- mcp1p is a novel microtubule plus-end tracking protein in fission yeast.
- mcp1p localization and transport are regulated by klp6p.
- mcp1p plays a role in microtubule destabilization.
- mcp1p and klp6p may function together to regulate microtubule dynamics at plus ends.
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