Abstract
To improve our understanding of the roles of microtubule cross-linking motors in mitosis, we analyzed two sea urchin embryonic kinesin-related proteins. It is striking to note that both of these proteins behave as homotetramers, but one behaves as a more compact molecule than the other. These observations suggest that these two presumptive motors could cross-link microtubules into bundles with different spacing. Both motors localize to mitotic spindles, and antibody microinjection experiments suggest that they have mitotic functions. Thus, one of these kinesin-related proteins may cross-link spindle microtubules into loose bundles that are 'tightened' by the other.
Original language | English (US) |
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Pages (from-to) | 38005-38011 |
Number of pages | 7 |
Journal | Journal of Biological Chemistry |
Volume | 275 |
Issue number | 48 |
DOIs | |
State | Published - Dec 1 2000 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology