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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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

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.[1]


  1. Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization. Lansbergen, G., Komarova, Y., Modesti, M., Wyman, C., Hoogenraad, C.C., Goodson, H.V., Lemaitre, R.P., Drechsel, D.N., van Munster, E., Gadella, T.W., Grosveld, F., Galjart, N., Borisy, G.G., Akhmanova, A. J. Cell Biol. (2004) [Pubmed]
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