| First Author | Lansbergen G | Year | 2004 |
| Journal | J Cell Biol | Volume | 166 |
| Issue | 7 | Pages | 1003-14 |
| PubMed ID | 15381688 | Mgi Jnum | J:93412 |
| Mgi Id | MGI:3057034 | Doi | 10.1083/jcb.200402082 |
| Citation | Lansbergen G, et al. (2004) Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization. J Cell Biol 166(7):1003-14 |
| abstractText | 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. |
