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© The Rockefeller University Press, 0021-9525/2000//851 $5.00
The Journal of Cell Biology, Volume 149, Number 4, , 2000 851-862

Original Article

Formation of Spindle Poles by Dynein/Dynactin-Dependent Transport of Numa



Andreas Merdesa, Rebecca Healdb, Kumiko Samejimaa, William C. Earnshawa, and Don W. Clevelandc

a ICMB, University of Edinburgh, Edinburgh EH9 3JR, Scotland
b Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, California 94720
c Ludwig Institute for Cancer Research and Division of Cellular and Molecular Medicine, University of California San Diego, La Jolla, California 92093-0660
ICMB, University of Edinburgh, King's Buildings, Edinburgh EH9 3JR, Scotland, UK.011 44 131 650 7360011 44 131 650 7075

a.merdes{at}ed.ac.uk

NuMA is a large nuclear protein whose relocation to the spindle poles is required for bipolar mitotic spindle assembly. We show here that this process depends on directed NuMA transport toward microtubule minus ends powered by cytoplasmic dynein and its activator dynactin. Upon nuclear envelope breakdown, large cytoplasmic aggregates of green fluorescent protein (GFP)-tagged NuMA stream poleward along spindle fibers in association with the actin-related protein 1 (Arp1) protein of the dynactin complex and cytoplasmic dynein. Immunoprecipitations and gel filtration demonstrate the assembly of a reversible, mitosis-spe-cific complex of NuMA with dynein and dynactin. NuMA transport is required for spindle pole assembly and maintenance, since disruption of the dynactin complex (by increasing the amount of the dynamitin subunit) or dynein function (with an antibody) strongly inhibits NuMA translocation and accumulation and disrupts spindle pole assembly.

Key Words: mitosis • microtubules • motor proteins • centrosome • spindle pole matrix

© 2000 The Rockefeller University Press

Abbreviations used in this paper: Arp1, actin-related protein 1; CSF, cytostatic factor; DAPI, 4',6'-diamidino-2-phenylindole; GFP, green fluorescent protein.


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