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Published 18 February 2003. doi:10.1083/jcb.200210021
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© The Rockefeller University Press, 0021-9525/2003/2/517 $5.00
The Journal of Cell Biology, Volume 160, Number 4, 517-528

Article

 The molecular function of Ase1p : evidence for a MAP-dependent midzone-specific spindle matrix



Scott C. Schuyler, Jenny Y. Liu and David Pellman

Department of Pediatric Oncology, The Dana-Farber Cancer Institute and Pediatric Hematology, The Children's Hospital, Harvard Medical School, Boston, MA 02115

Address correspondence to David Pellman, Dana-Farber Cancer Institute, 44 Binney St., Mayer 621A, Boston, MA 02115. Tel.: 617-632-4918. Fax: 617-632-5757. E-mail: david_pellman{at}dfci.harvard.edu

The midzone is the domain of the mitotic spindle that maintains spindle bipolarity during anaphase and generates forces required for spindle elongation (anaphase B). Although there is a clear role for microtubule (MT) motor proteins at the spindle midzone, less is known about how microtubule-associated proteins (MAPs) contribute to midzone organization and function. Here, we report that budding yeast Ase1p is a member of a conserved family of midzone-specific MAPs. By size exclusion chromatography and velocity sedimentation, both Ase1p in extracts and purified Ase1p behaved as a homodimer. Ase1p bound and bundled MTs in vitro. By live cell microscopy, loss of Ase1p resulted in a specific defect: premature spindle disassembly in mid-anaphase. Furthermore, when overexpressed, Ase1p was sufficient to trigger spindle elongation in S phase–arrested cells. FRAP revealed that Ase1p has both a very slow rate of turnover within the midzone and limited lateral diffusion along spindle MTs. We propose that Ase1p functions as an MT cross-bridge that imparts matrix-like characteristics to the midzone. MT-dependent networks of spindle midzone MAPs may be one molecular basis for the postulated spindle matrix.

Key Words: mitosis; microtubule-associated protein; spindle midzone; anaphase; budding yeast


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