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Originally published as MBC in Press, 10.1091/mbc.E04-12-1106 on August 24, 2005

Vol. 16, Issue 11, 5373-5384, November 2005

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Interactions between CLIP-170, Tubulin, and Microtubules: Implications for the Mechanism of CLIP-170 Plus-End Tracking Behavior{boxd}{boxv}

Eric S. Folker, Brian M. Baker, and Holly V. Goodson

Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46565

Submitted December 23, 2004; Revised August 9, 2005; Accepted August 17, 2005
Monitoring Editor: Ted Salmon

CLIP-170 belongs to a group of proteins (+TIPs) with the enigmatic ability to dynamically track growing microtubule plus-ends. CLIP-170 regulates microtubule dynamics in vivo and has been implicated in cargo-microtubule interactions in vivo and in vitro. Though plus-end tracking likely has intimate connections to +TIP function, little is known about the mechanism(s) by which this dynamic localization is achieved. Using a combination of biochemistry and live cell imaging, we provide evidence that CLIP-170 tracks microtubule plus-ends by a preassociation, copolymerization, and regulated release mechanism. As part of this analysis, we find that CLIP-170 has a stronger affinity for tubulin dimer than for polymer, and that CLIP-170 can distinguish between GTP- and GDP-like polymer. This work extends the previous analysis of CLIP-170 behavior in vivo and complements the existing fluorescence microscope characterization of CLIP-170 interactions with microtubules in vitro. In particular, these data explain observations that CLIP-170 localizes to newly polymerized microtubules in vitro but cannot track microtubule plus-ends in vitro. These observations have implications for the functions of CLIP-170 in regulating microtubule dynamics.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E04-12-1106) on August 24, 2005.

{boxd}{boxv} The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Address correspondence to: Holly V. Goodson (hgoodson{at}nd.edu).




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