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© The Rockefeller University Press, 0021-9525/1998//695 $5.00
The Journal of Cell Biology, Volume 143, Number 3, , 1998 695-707

Novel Features of the Light Chain of Microtubule-associated Protein MAP1B: Microtubule Stabilization, Self Interaction, Actin Filament Binding, and Regulation by the Heavy Chain

Institute of Biochemistry and Molecular Cell Biology, Vienna Biocenter, University of Vienna, A-1030 Vienna, Austria

Previous studies on the role of microtubule-associated protein 1B (MAP1B) in adapting microtubules for nerve cell-specific functions have examined the activity of the entire MAP1B protein complex consisting of heavy and light chains and revealed moderate effects on microtubule stability. Here we have analyzed the effects of the MAP1B light chain in the absence or presence of the heavy chain by immunofluorescence microscopy of transiently transfected cells. Distinct from all other MAPs, the MAP1B light chain–induced formation of stable but apparently flexible microtubules resistant to the effects of nocodazole and taxol. Light chain activity was inhibited by the heavy chain. In addition, the light chain was found to harbor an actin filament binding domain in its COOH terminus. By coimmunoprecipitation experiments using epitope-tagged fragments of MAP1B we showed that light chains can dimerize or oligomerize. Furthermore, we localized the domains for heavy chain–light chain interaction to regions containing sequences homologous to MAP1A. Our findings assign several crucial activities to the MAP1B light chain and suggest a new model for the mechanism of action of MAP1B in which the heavy chain might act as the regulatory subunit of the MAP1B complex to control light chain activity.

Key Words: microtubule-associated protein 1B • microtubules metabolism • nocodazole • actin stress fibers • cytoskeleton

Abbreviations used in this paper: HA, hemagglutinin; MAP, microtubule-associated protein.

Address all correspondence to Friedrich Propst, Institute of Biochemistry and Molecular Cell Biology, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria. Tel.: 43 1 4277 52858. Fax: 43 1 4277 52854. E-mail: friedrich.propst{at}univie.ac.at

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