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Papers In Press, published online ahead of print August 10, 2001
Physiology, University of Tennessee, Memphis, TN 38163
Corresponding Author: skhurana{at}utmem.edu
We have previously shown that tyrosine phosphorylation of the actin-regulatory protein villin is accompanied by the redistribution of phosphorylated villin and a concomitant decrease in the F-actin content of intestinal epithelial cells. The temporal and spatial correlation of these two events suggested that tyrosine phosphorylation of villin may be involved in the rearrangement of the microvillar cytoskeleton. This hypothesis was investigated by analyzing the effects of tyrosine phosphorylation of villin on the kinetics of actin polymerization by reconstituting in vitro the tyrosine phosphorylation of villin and its association with actin. Full-length recombinant human villin was phosphorylated in vitro by expression in the TKX1 competent cells that carry an inducible tyrosine kinase gene. The actin-binding properties of villin were examined using a co-sedimentation assay. Phosphorylation of villin did not change the stoichiometry (1:2), but decreased the binding affinity (4.4
J. Biol. Chem, 10.1074/jbc.C100418200
Submitted on July 25, 2001
Revised on August 8, 2001
Accepted on August 9, 2001
Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeleton
M for unphosphorylated vs. 0.6 M for phosphorylated) of villin for actin. Using a pyrene-actin based fluorescence assay, we demonstrated that tyrosine phosphorylation had a negative effect on actin nucleation by villin. In contrast, tyrosine phosphorylation enhanced actin severing by villin. Electron microscopic analysis showed complementary morphological changes. Phosphorylation inhibited the actin bundling and enhanced the actin severing functions of villin. Taken together our data show that tyrosine phosphorylation of villin decreased the amount of villin bound to actin filaments, inhibited the actin-polymerizing properties of villin and promoted the actin-depolymerizing functions instead. These observations suggest a role for tyrosine phosphorylation in modulating the microvillar cytoskeleton in vivo by villin in response to specific physiological stimuli.
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