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First published online January 17, 2003; 10.1105/tpc.008342

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The Plant Cell, Vol. 15, 303-315, February 2003, Copyright © 2003,
American Society of Plant Biologists

Misexpression of the Cyclin-Dependent Kinase Inhibitor ICK1/KRP1 in Single-Celled Arabidopsis Trichomes Reduces Endoreduplication and Cell Size and Induces Cell Death

Arp Schnittger1,2,a,b, Christina Weinlb,c, Daniel Bouyerb, Ulrike Schöbinger1,a,b and Martin Hülskamp2,b

a Zentrum für Molekularbiologie der Pflanzen, Universität Tübingen, Auf der Morgenstelle 3, 72076 Tübingen, Germany
b Botanisches Institut 3, Universität Köln, Gyrhofstrasse 15, 50931 Köln, Germany
c Unigruppe, Max-Planck-Institut für Züchtungsforschung, Carl von Linné Weg 10, 50829 Köln, Germany

2 To whom correspondence should be addressed. E-mail schnitt{at}mpiz-koeln.mpg.de; fax 49-0-221-5062-113; or e-mail martin.huelskamp{at}uni-koeln.mpg.de; fax 49-0-221-470-5062

A positive correlation between cell size and DNA content has been recognized in many plant cell types. Conversely, misexpression of a dominant-negative cyclin-dependent kinase (CDK) or CDK inhibitor proteins (ICK/KRPs) in Arabidopsis and tobacco leaves has revealed that cell growth can be uncoupled from cell cycle progression and DNA content. However, cell growth also appears to be controlled in a non-cell-autonomous manner by organ size, making it difficult in a ubiquitous expression assay to judge the cell-autonomous function of putative cell growth regulators. Here, we investigated the function of the CDK inhibitor ICK1/KRP1 on cell growth and differentiation independent of any compensatory influence of an organ context using Arabidopsis trichomes as a model system. By analyzing cell size with respect to DNA content, we dissected cell growth in a DNA-dependent and a DNA-independent process. We further found that ICK1/KRP1 misexpression interfered with differentiation and induced cell death, linking cell cycle progression, differentiation, and cell death in plants. The function of ICK1/KRP1 in planta was found to be dependent on a C-terminal domain and regulated negatively by an N-terminal domain. Finally, we identified CDKA;1 and a D-type cyclin as possible targets of ICK1/KRP1 expression in vivo.




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