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Updated: Jun 26, 2026

Using plusTipTracker Software to Measure Microtubule Dynamics in Xenopus laevis Growth Cones
Published on: September 7, 2014
EBs clip CLIPs to growing microtubule ends
1Department of Cell and Tissue Biology, University of California, San Francisco, San Francisco, CA 94143, USA. torsten.wittmann@ucsf.edu
Abstract:
Proteins that track growing microtubule (MT) ends are important for many aspects of intracellular MT function, but the mechanism by which these +TIPs accumulate at MT ends has been the subject of a long-standing controversy. In this issue, Bieling et al. (Bieling, P., S. Kandels-Lewis, I.A. Telley, J. van Dijk, C. Janke, and T. Surrey. 2008. J. Cell Biol. 183:1223-1233) reconstitute plus end tracking of EB1 and CLIP-170 in vitro, which demonstrates that CLIP-170 plus end tracking is EB1-dependent and that both +TIPs rapidly exchange between a soluble and a plus end-associated pool. This strongly supports the hypothesis that plus end tracking depends on a biochemical property of growing MT ends, and that the characteristic +TIP comets result from the generation of new +TIP binding sites through MT polymerization in combination with the exponential decay of these binding sites.
Insights
Plus-end tracking proteins (TIPs) accumulate at growing microtubule ends. This study shows CLIP-170 tracking depends on EB1, with both proteins rapidly exchanging between soluble and microtubule-associated pools.
Area of Science:
- Cell Biology
- Molecular Biology
Background:
- Plus-end tracking proteins (+TIPs) are crucial for microtubule dynamics and intracellular functions.
- The precise mechanism of +TIP accumulation at growing microtubule ends has been a long-standing debate.
Discussion:
- In vitro reconstitution demonstrates EB1-dependent plus-end tracking of CLIP-170.
- Both EB1 and CLIP-170 exhibit rapid exchange between soluble and microtubule-associated pools.
Key Insights:
- Plus-end tracking is influenced by the biochemical properties of growing microtubule ends.
- The characteristic comet-like appearance of +TIPs results from the continuous generation of new binding sites during microtubule polymerization and their subsequent decay.
Outlook:
- This work provides a mechanistic framework for understanding +TIP dynamics.
- Further research can explore the regulation of +TIP binding and dissociation at microtubule plus ends.
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