It has been previously shown that a class of microtubule proteins, the so-called microtubule-associated proteins (MAPs), binds to the C-terminal part of tubulin subunits. We show here that microtubules composed of tubulin whose 4-kDa C-terminal domain was cleaved by subtilisin (S-microtubules) are unable to bind MAPs but can still bind the anterograde translocator protein kinesin and the retrograde translocator dynein. Binding of both motors to S-microtubules, like their binding to normal microtubules, was ATP-dependent. In addition, direct competition experiments showed that binding sites for kinesin and MAPs on the microtubule surface lattice do not overlap. Furthermore, S-microtubules stimulated the ATPase activity of kinesin at least 8-fold, and the affinities of kinesin for control and S-microtubules were identical. S-microtubules were able to glide along kinesin-coated coverslips at a rate of 0.2 μm/s, the same rate as control microtubules. We conclude, that unlike MAPs, kinesin and cytoplasmic dynein bind to the tubulin molecule outside the C-terminal region.
|Original language||English (US)|
|Number of pages||6|
|Journal||Journal of Biological Chemistry|
|State||Published - Apr 25 1990|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology