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The Plant Cell, Vol. 13, 1929-1943, August 2001, Copyright © 2001,
American Society of Plant Biologists

Dynamic Recruitment of Cdc2 to Specific Microtubule Structures during Mitosis

Magdalena Weingartnera, Pavla Binarovab, Denisa Drykovab, Alois Schweighofera, Jean-Pierre Davidc, Erwin Heberle-Borsa, John Doonand and László Bögre1,e

a Institute of Microbiology and Genetics, University of Vienna, Vienna Biocenter, Dr. Bohrgasse 9, A-1030 Vienna, Austria
b Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídenská 1083, 142 20 Prague 4, Czech Republic
c Institute of Molecular Pathology, Dr. Bohrgasse 7, A-1030 Vienna, Austria
d Cell Biology Department, John Innes Centre, Norwich NR4 7UH, United Kingdom
e School of Biological Sciences, Royal Holloway, University of London, Egham TW20 OEX, United Kingdom

1 To whom correspondence should be addressed. E-mail l.bogre{at}rhul.ac.uk; fax 44-1784-434326

A-type cyclin-dependent kinases (CDKs), also known as cdc2, are central to the orderly progression of the cell cycle. We made a functional Green Fluorescent Protein (GFP) fusion with CDK-A (Cdc2-GFP) and followed its subcellular localization during the cell cycle in tobacco cells. During interphase, the Cdc2-GFP fusion protein was found in both the cytoplasm and the nucleus, where it was highly resistant to extraction. In premitotic cells, a bright and narrow equatorial band appeared on the cell surface, resembling the late preprophase band, which disintegrated within 10 min as followed by time-lapse images. Cdc2-GFP was not found on prophase spindles but left the chromatin soon after this stage and associated progressively with the metaphase spindle in a microtubule-dependent manner. Arresting cells in mitosis through the stabilization of microtubules by taxol further enhanced the spindle-localized pool of Cdc2-GFP. Toward the end of mitosis, Cdc2-GFP was found at the midzone of the anaphase spindle and phragmoplast; eventually, it became focused at the midline of these microtubule structures. In detergent-extracted cells, the Cdc2-GFP remained associated with mitotic structures. Retention on spindles was prevented by pretreatment with the CDK-specific inhibitor roscovitine and was enhanced by the protein phosphatase inhibitor okadaic acid. Furthermore, we demonstrate that both the endogenous CDK-A and Cdc2-GFP were cosedimented with taxol-stabilized plant microtubules from cell extracts and that Cdc2 activity was detected together with a fraction of polymerized tubulin. These data provide evidence that the A-type CDKs associate physically with mitotic structures in a microtubule-dependent manner and may be involved in regulating the behavior of specific microtubule arrays throughout mitosis.




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