The Ncd tail domain promotes microtubule assembly and stability

Citation
A. Karabay et Ra. Walker, The Ncd tail domain promotes microtubule assembly and stability, BIOC BIOP R, 258(1), 1999, pp. 39-43
Citations number
13
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006291X → ACNP
Volume
258
Issue
1
Year of publication
1999
Pages
39 - 43
Database
ISI
SICI code
0006-291X(19990429)258:1<39:TNTDPM>2.0.ZU;2-I
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 a s well as an ATP-dependent microtubule binding site in the C-terminal motor domain. The Ncd tail domain shares many properties with the microtubule-as sociated proteins that regulate microtubule assembly, including microtubule binding and bundling activity and an abundance of basic and proline residu es. Given these similarities, we examined the ability of Ncd tail domain pr oteins to promote MT assembly and stability. The results indicate that the Ncd tail domain can promote MT assembly and stabilize MTs against condition s that induce MT disassembly, and suggest that Ncd may influence MT dynamic s within the spindle. (C) 1999 Academic Press.