Abstract
Non-claret disjunctional (Ncd) is a Drosophila kinesin-like motor required for spindle assembly and maintenance in oocytes and early embryos. Ncd has an ATP-independent microtubule binding site in the N-terminal tail domain as well as an ATP-dependent microtubule binding site in the C-terminal motor domain. The Ncd tail domain shares many properties with the microtubule-associated proteins that regulate microtubule assembly, including microtubule binding and bundling activity and an abundance of basic and proline residues. Given these similarities, we examined the ability of Ncd tail domain proteins to promote MT assembly and stability. The results indicate that the Ncd tail domain can promote MT assembly and stabilize MTs against conditions that induce MT disassembly, and suggest that Ncd may influence MT dynamics within the spindle.
| Original language | English |
|---|---|
| Pages (from-to) | 39-43 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 258 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 29 Apr 1999 |
| Externally published | Yes |
Funding
This work was supported by an NIH grant (GM52340) (R.A.W.), a grant-in-aid of research from Sigma-Xi (A.K.), and a Graduate Research Development Project (GRDP) grant (A.K.) from the Graduate Student Assembly at Virginia Polytechnic Institute and State University. We are grateful to Bettina Deavours and Kali Phelps for their comments on this project and the manuscript.
| Funders | Funder number |
|---|---|
| State University | |
| National Institutes of Health | |
| National Institute of General Medical Sciences | R29GM052340 |
| Virginia Polytechnic Institute and State University |