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Vol. 10, Issue 5, 1521-1536, May 1999
and
*Howard Hughes Medical Institute, Center for Cancer Research,
Department of Biology, Massachusetts Institute of Technology,
Cambridge, Massachusetts 02139; and Fibroblasts, when plated on the extracellular matrix protein
fibronectin (FN), rapidly spread and form an organized actin cytoskeleton. This process is known to involve both the central Holland Laboratory,
American Red Cross, Rockville, Maryland 20855
5
1 integrin-binding and the C-terminal heparin-binding
regions of FN. We found that within the heparin-binding region, the
information necessary for inducing organization of stress fibers and
focal contacts was located in a 29-amino acid segment of FN type III module 13 (III13). We did not find a
cytoskeleton-organizing role for repeat III14, which had
previously been implicated in this process. Within III13,
the same five basic amino acids known to be most important for heparin
binding were also necessary for actin organization. A substrate of
III13 alone was only weakly adhesive but strongly induced
formation of filopodia and lamellipodia. Stress fiber formation
required a combination of III13 and III7-11 (which contains the integrin 51 recognition site), either
as a single fusion protein or as separate polypeptides, and the
relative amounts of the two binding sites appeared to determine whether stress fibers or filopodia and lamellipodia were the predominant actin
structures formed. We propose that a balance of signals from
III13 and from integrins regulates the type of
actin structures assembled by the cell.
Corresponding author. E-mail address:
rohynes{at}mit.edu.
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