| Autor: |
Askham, J. M., Vaughan, K. T., Goodson, H. V., Morrison, E. E. |
| Zdroj: |
Molecular Biology of the Cell; October 2002, Vol. 13 Issue: 10 p3627-3645, 19p |
| Abstrakt: |
EB1 is a microtubule tip–associated protein that interacts with the APC tumor suppressor protein and components of the dynein/dynactin complex. We have found that the C-terminal 50 and 84 amino acids (aa) of EB1 were sufficient to mediate the interactions with APC and dynactin, respectively. EB1 formed mutually exclusive complexes with APC and dynactin, and a direct interaction between EB1 and p150Gluedwas identified. EB1-GFP deletion mutants demonstrated a role for the N-terminus in mediating the EB1-microtubule interaction, whereas C-terminal regions contributed to both its microtubule tip localization and a centrosomal localization. Cells expressing the last 84 aa of EB1 fused to GFP (EB1-C84-GFP) displayed profound defects in microtubule organization and centrosomal anchoring. EB1-C84-GFP expression severely inhibited microtubule regrowth, focusing, and anchoring in transfected cells during recovery from nocodazole treatment. The recruitment of γ-tubulin and p150Gluedto centrosomes was also inhibited. None of these effects were seen in cells expressing the last 50 aa of EB1 fused to GFP. Furthermore, EB1-C84-GFP expression did not induce Golgi apparatus fragmentation. We propose that a functional interaction between EB1 and p150Gluedis required for microtubule minus end anchoring at centrosomes during the assembly and maintenance of a radial microtubule array. |
| Databáze: |
Supplemental Index |
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