Related Experiment Video
Updated: Aug 12, 2026

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
Published on: March 15, 2014
Dynamic localization of CLIP-170 to microtubule plus ends is coupled to microtubule assembly
G S Diamantopoulos1, F Perez, H V Goodson
1Department of Cell Biology, Sciences III, University of Geneva, CH-1211 Geneva 4, Switzerland. diamantopoulos@cellbio.unige.ch
Abstract:
CLIP-170 is a cytoplasmic linker protein that localizes to plus ends of microtubules in vivo. In this study, we have characterized the microtubule-binding properties of CLIP-170, to understand the mechanism of its plus end targeting. We show that the NH2-terminal microtubule-interacting domain of CLIP-170 alone localizes to microtubule plus ends when transfected into cells. Association of CLIP-170 with newly-formed microtubules was observed in cells microinjected with biotinylated tubulin, used as a tracer for growing microtubules. Using in vitro assays, association of CLIP-170 with recently polymerized tubulin is also seen. Cross-linking and sedimentation velocity experiments suggest association of CLIP-170 with nonpolymerized tubulin. We conclude from these experiments that the microtubule end targeting of CLIP-170 is closely linked to tubulin polymerization.
Related Concept Videos
Microtubule Instability
Microtubule Formation
Assembly of Complex Microtubule Structures
Microtubule Instability
Spindle Assembly
In most cells, centrosomes are the primary microtubule nucleation centers. In the centrosome-mediated pathway, the G2-prophase transition triggers centrosome maturation and increased microtubule nucleation. Progressive nucleation results in a microtubule array...
Anaphase A and B
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...

