Published 15 September 2003. doi:10.1083/jcb.200305143
© The Rockefeller University Press,
0021-9525/2003/9/1069 $5.00
The Journal of Cell Biology, Volume 162, Number 6, 1069-1077
Long continuous actin bundles in Drosophila bristles are constructed by overlapping short filaments
Gregory M. Guild,
Patricia S. Connelly,
Linda Ruggiero,
Kelly A. Vranich and
Lewis G. Tilney
Department of Biology, University of Pennsylvania, Philadelphia, PA 19104
Address correspondence to Gregory M. Guild, Dept. of Biology, University of Pennsylvania, Philadelphia, PA 19104-6018. Tel.: (215) 898-3433. Fax: (215) 898-8780. email: gguild{at}sas.upenn.edu
The actin bundles essential for Drosophila bristle elongation are hundreds of microns long and composed of cross-linked unipolar filaments. These long bundles are built from much shorter modules that graft together. Using both confocal and electron microscopy, we demonstrate that newly synthesized modules are short (12 µm in length); modules elongate to
3 µm by growing over the surface of longitudinally adjacent modules to form a graft; the grafted regions are initially secured by the forked protein cross-bridge and later by the fascin cross-bridge; actin bundles are smoothed by filament addition and appear continuous and without swellings; and in the absence of grafting, dramatic alterations in cell shape occur that substitutes cell width expansion for elongation. Thus, bundle morphogenesis has several components: module formation, elongation, grafting, and bundle smoothing. These actin bundles are much like a rope or cable, made by overlapping elements that run a small fraction of the overall length, and stiffened by cross-linking.
Key Words: cross-link; cytoskeleton; actin filaments; fascin protein; forked protein

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