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Journal Article

Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization.

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Lemaitre,  Regis P
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Drechsel,  David N
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Lansbergen, G., Komarova, Y., Modesti, M., Wyman, C., Hoogenraad, C. C., Goodson, H. V., et al. (2004). Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization. Journal of Cell Biology, 166(7), 1003-1014.


Cite as: https://hdl.handle.net/21.11116/0000-0001-121F-9
Abstract
Cytoplasmic linker protein (CLIP)-170, CLIP-115, and the dynactin subunit p150(Glued) are structurally related proteins, which associate specifically with the ends of growing microtubules (MTs). Here, we show that down-regulation of CLIP-170 by RNA interference results in a strongly reduced accumulation of dynactin at the MT tips. The NH(2) terminus of p150(Glued) binds directly to the COOH terminus of CLIP-170 through its second metal-binding motif. p150(Glued) and LIS1, a dynein-associating protein, compete for the interaction with the CLIP-170 COOH terminus, suggesting that LIS1 can act to release dynactin from the MT tips. We also show that the NH(2)-terminal part of CLIP-170 itself associates with the CLIP-170 COOH terminus through its first metal-binding motif. By using scanning force microscopy and fluorescence resonance energy transfer-based experiments we provide evidence for an intramolecular interaction between the NH(2) and COOH termini of CLIP-170. This interaction interferes with the binding of the CLIP-170 to MTs. We propose that conformational changes in CLIP-170 are important for binding to dynactin, LIS1, and the MT tips.