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Plant Cell, Vol. 12, 979-990, June 2000, Copyright © 2000, American Society of Plant Physiologists

The Kinesin-like Calmodulin Binding Protein Is Differentially Involved in Cell Division

Jan W. Vosa, Farida Safadib, Anireddy S. N. Reddyb, and Peter K. Heplera
a Biology Department, University of Massachusetts, Amherst, Massachusetts 01003
b Department of Biology, Colorado State University, Fort Collins, Colorado 80523

Correspondence to: Jan W. Vos, Present address and address for correspondence: Laboratory for Experimental Plant Morphology and Cell Biology, Wageningen University, Arboretumlaan 4, 6703 BD Wageningen, The Netherlands., jan.vos{at}algem.pcm.wau.nl (E-mail), 31-317-485005 (fax)

The kinesin-like calmodulin (CaM) binding protein (KCBP), a minus end–directed microtubule motor protein unique to plants, has been implicated in cell division. KCBP is negatively regulated by Ca2+ and CaM, and antibodies raised against the CaM binding region inhibit CaM binding to KCBP in vitro; therefore, these antibodies can be used to activate KCBP constitutively. Injection of these antibodies into Tradescantia virginiana stamen hair cells during late prophase induces breakdown of the nuclear envelope within 2 to 10 min and leads the cell into prometaphase. However, mitosis is arrested, and the cell does not progress into anaphase. Injection of antibodies later during cell division has no effect on anaphase transition but causes aberrant phragmoplast formation and delays the completion of cytokinesis by ~15 min. These effects are achieved without any apparent degradation of the microtubule cytoskeleton. We propose that during nuclear envelope breakdown and anaphase, activated KCBP promotes the formation of a converging bipolar spindle by sliding and bundling microtubules. During metaphase and telophase, we suggest that its activity is downregulated.


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