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Curr Biol. 2004 Dec 14;14(23):2086-95.

CLIP-170/tubulin-curved oligomers coassemble at microtubule ends and promote rescues.

Author information

1
Equipe Structure et Dynamique des Macromolécules, Unité Mixte de Recherche 6026, Centre National de la Recherche Scientifique, Université de Rennes 1, Campus de Beaulieu, 35042 Rennes Cedex, France. isabelle.arnal@univ-rennes1.fr

Abstract

BACKGROUND:

CLIP-170 is a microtubule binding protein specifically located at microtubule plus ends, where it modulates their dynamic properties and their interactions with intracellular organelles. The mechanism by which CLIP-170 is targeted to microtubule ends remains unclear today, as well as its precise effect on microtubule dynamics.

RESULTS:

We used the N-terminal part of CLIP-170 (named H2), which contains the microtubule binding domains, to investigate how it modulates in vitro microtubule dynamics and structure. We found that H2 primarily promoted rescues (transitions from shrinkage to growth) of microtubules nucleated from pure tubulin and isolated centrosomes, and stimulated microtubule nucleation. Electron cryomicroscopy revealed that H2 induced the formation of tubulin rings in solution and curved oligomers at the extremities of microtubules in assembly conditions.

CONCLUSIONS:

These results suggest that CLIP-170 targets specifically at microtubule plus ends by copolymerizing with tubulin and modulates microtubule nucleation, polymerization, and rescues by the same basic mechanism with tubulin oligomers as intermediates.

PMID:
15589150
DOI:
10.1016/j.cub.2004.11.055
[Indexed for MEDLINE]
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