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Vol. 10, Issue 12, 4201-4215, December 1999
and
*Howard Hughes Medical Institute and Department of Cell Biology,
Vanderbilt University School of Medicine, Nashville, Tennessee 37232;
and The Arp2/3 complex is an essential component of the yeast actin
cytoskeleton that localizes to cortical actin patches. We have isolated
and characterized a temperature-sensitive mutant of
Schizosaccharomyces pombe arp2 that displays a defect in
cortical actin patch distribution. The arp2+
gene encodes an essential actin-related protein that colocalizes with
actin at the cortical actin patch. Sucrose gradient analysis of the
Arp2/3 complex in the arp2-1 mutant indicated
that the Arp2p and Arc18p subunits are specifically lost from the
complex at restrictive temperature. These results are consistent with immunolocalization studies of the mutant that show that Arp2-1p is
diffusely localized in the cytoplasm at restrictive temperature. Interestingly, Arp3p remains localized to the cortical actin patch under the same restrictive conditions, leading to the hypothesis that
loss of Arp2p from the actin patch affects patch motility but does not
severely compromise its architecture. Analysis of the mutant Arp2
protein demonstrated defects in ATP and Arp3p binding, suggesting a
possible model for disruption of the complex.
Department of Molecular, Cellular, and Developmental
Biology, University of Colorado, Boulder, Colorado 80309-0347
Corresponding author. E-mail address:
jenny.morrell{at}mcmail.vanderbilt.edu.
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