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

doi:10.1083/jcb.143.3.695

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J. Cell Biol., Volume 143, Number 3, November 2, 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

Martin Tögel, Gerhard Wiche, and Friedrich Propst

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-specificfunctions have examined the activity of the entire MAP1B proteincomplex consisting of heavy and light chains and revealed moderateeffects on microtubule stability. Here we have analyzed the effectsof the MAP1B light chain in the absence or presence of the heavychain by immunofluorescence microscopy of transiently transfectedcells. Distinct from all other MAPs, the MAP1B light chain-inducedformation of stable but apparently flexible microtubules resistantto the effects of nocodazole and taxol. Light chain activity wasinhibited by the heavy chain. In addition, the light chain wasfound to harbor an actin filament binding domain in its COOH terminus.By coimmunoprecipitation experiments using epitope-tagged fragmentsof MAP1B we showed that light chains can dimerize or oligomerize.Furthermore, we localized the domains for heavy chain-light chaininteraction to regions containing sequences homologous to MAP1A.Our findings assign several crucial activities to the MAP1B lightchain and suggest a new model for the mechanism of action of MAP1Bin which the heavy chain might act as the regulatory subunit ofthe MAP1B complex to control light chain activity.

Key words: microtubule-associated protein 1B; microtubules metabolism; nocodazole; actin stress fibers; cytoskeleton

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