Plant Physiology 132:2034-2044 (2003)
© 2003 American Society of Plant Biologists
CELL BIOLOGY AND SIGNAL TRANSDUCTION
The Putative Arabidopsis Arp2/3 Complex Controls Leaf Cell Morphogenesis1,[w]
Shundai Li,
Laurent Blanchoin,
Zhenbiao Yang and
Elizabeth M. Lord*
Department of Botany and Plant Sciences and Center for Plant Cell
Biology, University of California, Riverside, California 92521 (S.L., Z.Y.,
E.M.L.); and Laboratoire de Physiologie Cellulaire Végétale,
Centre National de la Recherche Scientifique, 17 rue des martyrs, 38054
Grenoble, France (L.B.)
The evolutionarily conserved Arp2/3 complex has been shown to activate
actin nucleation and branching in several eukaryotes, but its biological
functions are not well understood in multicellular organisms. The model plant
Arabidopsis provides many advantages for genetic dissection of the function of
this conserved actin-nucleating machinery, yet the existence of this complex
in plants has not been determined. We have identified Arabidopsis genes
encoding homologs of all of the seven Arp2/3 subunits. The function of the
putative Arabidopsis Arp2/3 complex has been studied using four homozygous
T-DNA insertion mutants for ARP2, ARP3, and
ARPC5/p16. All four mutants display identical defects in the
development of jigsaw-shaped epidermal pavement cells and branched trichomes
in the leaf. These loss-of-function mutations cause mislocalization of diffuse
cortical F-actin to the neck region and inhibit lobe extension in pavement
cells. The mutant trichomes resemble those treated with the
actin-depolymerizing drug cytochalasin D, exhibiting stunted branches but
dramatically enlarged stalks due to depolarized growth suggesting defects in
the formation of a fine actin network. Our data demonstrate that the putative
Arabidopsis Arp2/3 complex controls cell morphogenesis through its roles in
cell polarity establishment and polar cell expansion. Furthermore, our data
suggest a novel function for the putative Arp2/3 complex in the modulation of
the spatial distribution of cortical F-actin and provide evidence that the
putative Arp2/3 complex may activate the polymerization of some types of actin
filaments in specific cell types.
1 This work was supported by the National Science Foundation (grant nos.
IBN–0115078 and MCB–0111082 to Z.Y. and IBN 0077886 to
E.M.L.).
[w] The online version of this article contains Web-only data. The supplemental
material is available at
http://www.plantphysiol.org.
*
Corresponding author; e-mail
lord{at}citrus.ucr.edu;
fax 909–787–4437.
Received June 13, 2003;
returned for revision June 15, 2003;
accepted June 16, 2003.
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