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© The Rockefeller University Press, 0021-9525/1998//159 $5.00
The Journal of Cell Biology, Volume 143, Number 1, , 1998 159-170

Regular Articles

Rapid Movements of Vimentin on Microtubule Tracks: Kinesin-dependent Assembly of Intermediate Filament Networks



Veena Prahlad*, Miri Yoon*, Robert D. Moir*, Ronald D. Vale{ddagger}, and Robert D. Goldman*

* Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611; and {ddagger} Howard Hughes Medical Institute, University of California, San Francisco, California 94143

The assembly and maintenance of an extended intermediate filament (IF) network in fibroblasts requires microtubule (MT) integrity. Using a green fluorescent protein–vimentin construct, and spreading BHK-21 cells as a model system to study IF–MT interactions, we have discovered a novel mechanism involved in the assembly of the vimentin IF cytoskeleton. This entails the rapid, discontinuous, and MT-dependent movement of IF precursors towards the peripheral regions of the cytoplasm where they appear to assemble into short fibrils. These precursors, or vimentin dots, move at speeds averaging 0.55 ± 0.24 µm/s. The vimentin dots colocalize with MT and their motility is inhibited after treatment with nocodazole.

Our studies further implicate a conventional kinesin in the movement of the vimentin dots. The dots colocalize with conventional kinesin as shown by indirect immunofluorescence, and IF preparations from spreading cells are enriched in kinesin. Furthermore, microinjection of kinesin antibodies into spreading cells prevents the assembly of an extended IF network. These studies provide insights into the interactions between the IF and MT systems. They also suggest a role for conventional kinesin in the distribution of non-membranous protein cargo, and the local regulation of IF assembly.

Key Words: intermediate filaments • vimentin • microtubule • kinesin • cytoskeleton

Abbreviations used in this paper: GFP, green fluorescent protein; IF, intermediate filaments; MT, microtubules; TX-100, Triton X-100.

Address all correspondence to Robert D. Goldman, Department of Cell and Molecular Biology, Northwestern University Medical School, 303 E. Chicago Ave., Chicago, IL 60611. Tel.: (312) 503-4215. Fax: (312) 503-0954. E-mail: r-goldman{at}nwu.edu


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